Citation: Albert W. Pilkington IV, Justin Legleiter. Challenges in understanding the structure/activity relationship of Aβ oligomers[J]. AIMS Biophysics, 2019, 6(1): 1-22. doi: 10.3934/biophy.2019.1.1
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The development of new materials is often the beginning of innovative and future-oriented technologies. This is necessary to meet tomorrow’s engineering applications, for example, to increase efficiency, reliability and productivity or to reduce energy consumption and with this to raise standard of living [1,2].
It is also possible to understand the term“new material”as a combination of materials. Joining metals and ceramics for example, allows the combination of the positive properties of both. Metallic materials offer magnetic properties, a high ductility or an electrical conductivity, while ceramic materials have a high strength even at elevated temperatures, a high corrosion resistance and, in the case of zirconia, an oxygen-ion conductivity.
These combinations are necessary in solid oxide fuel cells, gas separation membranes, thermoelectric generators, bipolar surgical tools or in mechanical engineering applications. Major obstacle for using these composites is, that existing manufacturing technologies cannot fulfil requirements in terms of costs, complex geometries or operation conditions.
Conventional frictional and form-locking joining techniques, like screwing or shrinking, offer a simple possibility to combine both materials. However, these joining techniques have many disadvantages regarding wall thicknesses and geometrical design.
Conventional cohesive joining techniques, like gluing or brazing, allow chemical bonding between both materials. Especially gluing allows a simple joining, while for brazing a special development of brazing material is necessary [3]. However, within both processes a further material is inserted which can limit functionality, operation temperature or strength. Nevertheless, brazing is already well established for joining power electronics or stacks of solid oxide fuel cells.
It is generally known that in addition to conventional joining techniques several powder technological approaches exist. One of these approaches is thermal spraying. This is used for applying a metallic or ceramic layer on top of ceramic or metallic substrate [4]. This allows the production of electrical circuits on insulating substrates, wear-resistant layers or thermal barrier coatings. Layer thicknesses thereby range from 30 µm to some millimetres. The high layer thickness is a disadvantage as well as the high porosity and high surface roughness. Furthermore, the coating of complex geometries is quite difficult.
One promising approach to simplify the production of composites and achieving a high degree of freedom regarding design is a co-shaping, continued with co-sintering. Especially the co-sintering step is the challenge of this manufacturing route. Differences in coefficient of thermal expansion (CTE) or in densifying behaviour (shrinkage) can lead to stresses during heating or cooling [5]. These stresses can cause flaws as cracks, delaminations, pores, changes in microstructure or in the case of asymmetric composites a warpage. Cai et al. has theoretically analysed occurring stresses during sintering of composites [5]. He considered that the materials exhibit during sintering pure viscous behaviour and developed, based on this assumption, equations for maximum stresses σK in bi-layered asymmetric (equation 1) and three-layered symmetric (equation 2) composites.
${\sigma _K}=[\frac{{{m^4} + mn}}{{{n^2} + 2mn(2{m^2} + 3m + 2 + {m^{(4)}})}}]\eta \Delta \dot \varepsilon $ | (1) |
${\sigma _K}=\frac{1}{{1 + m n}}\eta \Delta \dot \varepsilon $ | (2) |
Especially his equation for the rate of warping (equation 3), which was derived from equation 1, is commonly used for a comparison of theory and practice [6,7,8].
$\dot k=\frac{{6{{(m + 1)}^2}m n}}{{{m^4}{n^2} + 2mn(2{m^2} + 3m + 2) + 1}}\Delta \dot \varepsilon $ | (3) |
It can be derived from these equations that besides of the difference in CTE and sintering behaviour, which is represented as difference in sintering strain rate $\Delta \dot \varepsiloṅ$, the ratio of layer thickness m and the material viscosity η respectively ratio of the material viscosities n influence stresses and warpage.
Furthermore, it is known that non-or low-shrinking substrates can harm and slow down densifying of thin ceramic layers during co-sintering, which result in lower densities in comparison to free shrinking materials [9,10,11]. In this context Yamaguchi et al. and Muecke et al. showed that high densities in co-sintered ceramic layers can only be reached, if differences in strain rate are small enough or if the negative effect is compensated by an increased isothermal dwell time [11,12].
The first step to avoid flaws during co-sintering is the choice of materials with well adapted CTE’s. The second step is the reduction of mismatches in sintering strain rate. The main focus of investigations for the second step is the adaptation of green densities, use of specific particle sizes, changing heating rates, using doping elements or integrating a material gradient [13,14,15,16,17]. In this work, sintering behaviour was influenced and adjusted by treating metallic powder with a high energy milling step [18,19].
The aim of this work was to achieve a multi-layered composite consisting of a thin ceramic layer on top or between two thicker porous metallic layers. These composites are suitable as semi-finished metal supported fuel cells, filter elements or gas separation membranes. Thereby, investigations about the co-sintering behaviour of adapted and un-adapted composites were done. A combination of zirconia and stainless steel as materials was used. The composites were produced by using a tape casting process, which is the standard process in ceramic industry for the production of large-area, thin and flat ceramic substrates [20].
For the investigations 3 mol% yttrium stabilized zirconia TZ-3YS-E (Tosoh Inc., Japan) was selected as ceramic material and the gas atomized high temperature corrosion resistant ferritic iron-chromium alloy Crofer®22APU (H. C. Starck GmbH, Germany) as metallic one. The metallic powder was treated with a high energy milling step, to influence its sintering behaviour. Further information about this can be found in earlier publications [18,19,21]. Overall, four different metallic powders (metal powder 1-4) were taken, which differentiate in terms of their sintering behaviour. Crofer®22APU was chosen due to its melting temperature of 1510°C which is above the sintering temperature of 1450°C of the zirconia powder.
Different metal-ceramic (asymmetric) and metal-ceramic-metal (symmetric) composites were produced by tape casting. For this a slurry consisting of water, polyvinylalcohol as binder and glycerine as plasticizer was prepared. Polyvinylalcohol and glycerine were taken due to their good decomposition behaviour under hydrogen atmosphere, which is important to avoid a harmful increase of carbon content in steel after sintering [22]. Besides binder and plasticizer, the defoamer Foammaster F111 (BASF SE, Germany) and the surfactant Glycol N 109 (Zschimmer & Schwarz GmbH % Co. KG, Germany) were used. The composition of the individual slurries is shown in table 1. More details concerning the production process are published in [18,22,23].
powder | water | binder | plasticizer | de-foamer | surfactant | |
TZ-3YS-E | 44.5 | 45.1 | 4.3 | 5.7 | 0.2 | 0.2 |
metal powder 1 | 43.3 | 35.7 | 4.3 | 6.5 | 0.1 | 0.1 |
metal powder 2 | 80.5 | 15.6 | 1.6 | 2 | 0.1 | 0.2 |
metal powder 3 | 65.3 | 28.1 | 3 | 3.3 | 0.1 | 0.2 |
metal powder 4 | 80.5 | 15.6 | 1.6 | 2 | 0.1 | 0.2 |
Tape casting allows the production of asymmetric and symmetric composites. Asymmetric composites were produced with the combination TZ-3Y-SE and metal powder 1 (composite 1a) respectively powder 2 (composite 2). Symmetric composites were produced with metal powder 3 (composite 3), powder 4 (composite 4) and again with powder 1 (composite 1s). The ceramic green layer thickness was in all cases 11.6±1 µm while the metallic layer thickness varied from 200 to 400 µm. Hence, the metallic layer thickness is 17 to 34 times thicker than the ceramic one. It has to be noted that the specific metallic layer thickness has no influence on the shown results, for which reason it is not specified in detail. Figure 1 exhibits an asymmetric metal-ceramic multi-layered green tape out of composite 2. The ceramic layer thickness was measured before and after sintering using field emission electron scanning microscopy (FESEM) (NVision 40, Carl Zeiss SMT GmbH, Germany).
Round specimens with a diameter of 20 mm were punched out of the tapes for co-sintering experiments. These tapes were debinded and sintered on top and between two porous, 1 mm thick Keralpor 99 alumina sintering supports (Kerafol Keramische Folien GmbH, Germany) respectively. Covering the tapes with a sintering support was necessary to avoid warpage during sintering. Furthermore, two smaller specimens with a rectangular shape and dimensions of 5×7 mm out of composite 1a and 2 were sintered without a coverage.
The specimens were debinded under hydrogen atmosphere with a heating rate of 1 K/min up to 600°C. After a dwell time of 2 h the furnace (RRO280/300-900V, MUT advanced heating, Germany) was cooled down to room temperature with a rate of 3 K/min. Sintering took place in a separated furnace (HTBL20W22-2G, Carbolite Gero GmbH & Co. KG, Germany) with a heating rate of 3 K/min up to the sintering temperature between 1200 and 1400°C and a cooling rate of 4 K/min. The dwell time was 2 h and the sintering atmosphere was a mixture of argon (80%) and hydrogen (20%).
The sintering behaviour of the materials was characterized with high temperature heating microscope (EHM 201-17K, Hesse Instruments, Germany). Thereby a camera records pictures of the specimen during sintering in a tube furnace. A following image analyses allows a calculation of linear shrinkage as well as sintering strain rate. During this measurement the tube furnace was flushed with gas (95% argon, 5% hydrogen). Heating rate was 1 K/min up to 600°C and then 3 K/min up to 1400°C. The used specimens were 1 mm in thickness and had a diameter of 5 mm. Using a heating microscope instead of pushing rod dilatometer, had the advantage to get free shrinkage curves of the materials. When using a pushing rod dilatometer, the pressure of the pushing rod can especially falsify the measurement of the metallic material due to its low viscosity at high temperatures.
The pushing rod dilatometer Dil 402 D (Netsch Gerätebau GmbH, Germany) was used for measuring the CTEs. The CTE was measured by means of sintered laminates (density > 99%) of each material with dimensions of 4×4×20 mm3.
The sintered composites were cut in the middle and were prepared by grinding and polishing with abrasive papers for microstructural investigations with the field emission scanning microscope NVision 40 (Carl Zeiss SMT GmbH, Germany), . The green tapes, however, were prepared using broad ion beam method. 10-15 pictures with a magnification of 7000 and a backscattered electron detector, which shows the material contrast, were taken to analyse porosity. The porosity was afterwards determined by image analysing with the software ImageJ V1.6.0 (National Institute of Health, USA).
The viscosity of the ceramic and metallic materials during sintering was measured using the bending beam method. This method is usually used to measure the viscosity of glasses [24] but was adapted by Lee et al. [25] and Lame et al. [26] to measure the viscosity of oxide ceramics and steels during sintering. Thereby, a beam is sintered on top of a special support which has only two contact points at the left and right side of the tape. It is then possible to calculate the viscosity η from the rate of deflection ${\dot \delta }$ using equation 4 [27].
$\eta=\frac{{5{\text{ }}\rho g {L^4}}}{{32{\text{ }}\dot \delta {h^2}}}$ | (4) |
The span length L during the measurements amounted 10 mm. After preliminary tests, the thickness h of the tapes was set to 100 µm for the ceramic and 500 µm for the metallic. These tapes were pre-sintered up to 1000°C to avoid a bending during de-binding and to give the tapes some strength.
Before and after co-sintering, the ceramic layer of the asymmetric composites was investigated in terms of its phase composition by using x-ray diffraction (Bruker D8 ID 3003TT, Bruker Corporation, USA).
The tensile adhesive strength between the ceramic and metallic layers was measured using the symmetric structured composite 1s and, furthermore, composites with dense metallic layers. The powder treatment and the composition for the dense sintering metallic tapes is published in [19]. For testing round specimens with a diameter of approximately 25 mm (after sintering) were prepared and sintered at 1270, 1330 and 1400°C. The test was carried out in accordance to DIN EN 582 with a velocity of 0.5 mm/min [28]. It is known from Dourandish et al. [29] that boron can increase tensile strength of composites, due to the formation of a Fe-B eutectic at 1170°C, which enables an improved wetting of the ceramic material. To investigate this 0.03 and 0.63 wt% amorphous boron was added to the ceramic layer. The test was done with a 100 kN universal testing machine (Zwick GmbH, Germany) (figure 2). For this, the metallic layers were glued to the testing stamps with FM®1000 gluing pads (Cytec Industries Corp., USA).
Figure 3 shows the CTE of the used materials up to a temperature of 1200°C. CTEs match well to each other until 700°C, with a maximum mismatch below 1.0×10−6 1/K. With increasing temperature especially the CTE of the metallic material increases, which leads to a mismatch of 2.4×10−6 1/K at 1200°C [18]. However, it has to be assumed that the gap between the CTEs at higher temperatures isn’t as bad as at lower temperatures because the metallic material has a low elasticity/viscosity at higher temperatures. Hence, the metallic layer can absorb some occurring stresses by deformation. Furthermore, other metallic materials and especially the austenitic steels 17-4PH or 316L, which are often used for the combination with zirconia, have much higher CTE’s and with this, higher mismatches [30].
Figure 4 compares the sintering behaviour of ceramic and the four different metallic powders as a function of temperature and dwell time. The TZ-3YS-E powder starts sintering at 1150°C. Its linear shrinkage at the end of the dwell time amounts 23.5%.
Metal powder 1 starts sintering in the same temperature region (1150°C) as the TZ-3YS-E. Hereby, also the course of shrinkage exhibits a good agreement until the beginning of the dwell time. This leads to a good accordance of the sintering strain rates (figure 5) and, furthermore, only a small maximum mismatch in strain rate of±0.25×10−3 1/min (figure 6) until the beginning of the dwell time. The mismatch in strain rate increases up to a maximum value of −0.75×10−3 1/min due to the lower strain rate of metal powder 1 in the first 30 minutes of the dwell time.
In comparison to powder 1, all other metallic powders start sintering at higher temperatures. Furthermore, their strain rates are significantly lower which results in lower total shrinkage values of 16.5% for powder 2, 10% for powder 3 and 7.5% for powder 4, respectively.
The later onset of sintering, as well as the lower maximum sintering strain rates, result in higher differences in strain rate. Composite 3 has a maximum mismatch at 1280°C of −2×10−3 1/min, while composite 2 and 4 have the highest mismatch values at −3×10−3 1/min (figure 6).
Figure 7 presents FESEM images of the microstructure of pure 1000 µm thick zirconia tapes after sintering for 2 h at 1350 and 1400°C. Analysis exhibited that the porosity at 1350°C amounts 4.2%, while increasing sintering temperature to 1400°C decreases porosity below 1%.
The asymmetric composites 1a and 2 were sintered with and without a coverage. While the mismatches in strain rate led to a warpage of the uncovered composites (figure 8), the coverage completely avoided a warpage. Thereby the coverage led to no macroscopic cracks on the surface of the composites. Considering figure 8, it is visible that the higher mismatch in strain rate of composite 2 in comparison to composite 1a led to a more significant warpage, despite its higher metallic layer thickness.
It is reducible to differences in viscosity that the much thinner ceramic layer (green thickness 11.6 µm) can bend the whole composite with a metallic layer thickness between 200 µm (composite 1a) and 400 µm (composite 2). Figure 9 shows the temperature-and density-dependent viscosity of the ceramic layer and metal powder 1 during sintering. The ceramic material starts with a viscosity of 1100 GPa*s at 1150°C. At lower temperatures, the viscosity was too high so that no measurements were possible. With increasing sintering temperature, viscosity decreased to 20 GPa*s. During dwell time, further sintering and densification led to an increase of the viscosity up to 250 GPa*s. The same response exhibits the metallic material, whereby its viscosity is the whole time 1 to 2 magnitudes lower, which is the reason for that the thin ceramic layer can bend the whole composite. The measured viscosity values, thereby match well with already published values from literature (24, 25).
Figure 10 shows the porosity of the free sintered ceramic layer (TZ-3YS-E) as well as the porosity of the co-sintered ceramic layers of composite 1a and 2 at different temperatures with a dwell time of 2h, covered and uncovered. Comparing porosities of the uncovered composites at 1350°C with the free sintered zirconia layer, it is obvious that the sintering behaviour of the zirconia layer is influenced by the metallic substrate. The porosity of composite 2 amounts 7.5%, which is 3% higher than the porosity of the free sintered zirconia layer, while the porosity of composite 1a is 1.5% lower than the porosity of the free sintered layer. This is caused by compression stresses (composite 1a) and tensile forces (composite 2), respectively, which improve respectively reduce sinter activity of the zirconia layer.
The negative influence is increased when the composite is covered during sintering. In this case, tensions cannot be prevented or relieved by a warping of the composite. Regarding the covered composite 2, it shows already at 1200°C an 8% higher porosity than the free sintered layer. With increasing sintering temperature the mismatch is slightly increased up to 9%. Comparisons of the covered and uncovered composites show that the porosity is 4% higher when it is covered during sintering. In contrast to these results, the coverage shows no negative influence in the case of composite 1. Here, both ceramic layers have porosities around 1%.
Further investigations, using symmetric structured composites out of the combination 1s, 3 and 4, confirm these results (figure 11). After sintering at 1350°C, the porosity of the zirconia layer of composite 3 and 4 amount 11%, respectively 15%, while composite 1s has a porosity of 2%. The porosity of composite4 is higher than the porosity of composite 3, due to its lower lateral shrinkage.
Nevertheless, an increase of the sintering temperature up to 1400°C minimizes the negative effect of the metallic layers on densification of zirconia layers. At this temperature, the porosity is in all cases below 1%. This is also visible in the scanning microscopy images of the composites in figure 12 on the right hand side.
The lateral shrinkage of the ceramic layers in the case of composite 3 and 4 is constraint due to the metallic substrate. Accordingly, densification of the ceramic layer at 1400°C is only possible with an increased shrinkage in thickness direction. This is evidenced by measurements of the thickness before and after sintering (table 2). In green state the ceramic layer thickness amounts in all cases 11.6 µm. At 1400°C the ceramic layer thickness is between 9.5 and 8.2 µm, depending on the composite composition. Composite 1s has the biggest layer thickness after sintering, because the metallic substrate has nearly the same lateral shrinkage as the pure zirconia layer. This leads to a calculated shrinkage in thickness-direction of 18.1%. In the case of composite 3 and 4 the metallic layers have lower lateral shrinkage values, which leads to an increased shrinkage in z-direction of 27% and 29% respectively.
composite | green | 1400 °C | |
layer thickness/µm | layer thickness/µm | shrinkage/% | |
1 | 9.5 ± 1.4 | 18.1 | |
3 | 11.6 ± 1.0 | 8.5 ± 1.4 | 26.7 |
4 | 8.2 ± 1.2 | 29.3 |
The results show that it is possible to densify the zirconia layer, even in combination with a high mismatch in strain rate. Despite these results, an adaptation of the sintering behaviour is indispensable. This is visible in the FESEM-images with lower magnifications (left hand side and middle in figure 12). While composite 1s has a completely defect free zirconia layer which is necessary for the different applications, sintering of both other composites is possible but they exhibit (micro-) cracks in the ceramic layer. Hence, a good adaption of sintering behaviour is necessary to achieve defect free composites.
Figure 13 shows x-ray diffraction measurements of the zirconia layer of composite 1a before and after sintering. As the measurements show, before sintering the powder has some monoclinic phases which are non-existent after sintering. This result is independent of the investigated composite (composite 1a or 2) and demonstrates that a mismatch in CTE above 700°C, does not lead to a stress induced transformation of the tetragonal in the monoclinic phase.
The formation of mixed oxide phases [18] as well as a mechanical grouting is the bases of bonding between both materials.
Figure 14 left shows a metal-ceramic-metal composite consisting of a dense metallic layer (porosity < 3%) in combination with the zirconia layer. As the higher magnification at the right side of the figures shows, there is a 0.5 µm thick mixed oxide phase in the interface of both materials. The EDX measurement of this phase shows, that in addition to the main elements of both materials there exist an accumulation of different alloying elements as Al, La, Si. These elements can form phases as La2O3, AlLaO3 or for example ZrSiO4.
Measurements of the adhesive tensile strength of composite 1s (porous metallic layer) exhibit a high dependency on sintering temperature (figure 15). Starting with a tensile strength between 1 and 2 MPa at 1270°C it is increased up to 4-5 MPa at 1330°C. Thereby, also a slight increase of the strength with increased boron content is visible. An increase of the sintering temperature up to 1400°C doubled tensile strength to 8 MPa without boron. Hereby, the strongest influence of the boron content is visible with an increase up to 9.6 MPa with 0.03% boron and up to 10.8 MPa with 0.63%. Regarding the use of boron, it has to be assumed that boron can lead to the formation of glass phases in the zirconia material which can negatively influence its properties. So, according to the specific application, the use of boron has to be reconsidered.
The experiments exhibited that the composite breaks preferably at one metal ceramic interface, while the ceramic layer stays intact. This is visible in figure 16, which shows a top view on the ceramic layer after tensile tests. Some metallic particles are on top of the ceramic layer, which were pulled out of the metallic layer.
Against the expectation tests of composites with dense metallic layers, sintered for 2 h at 1400°C, showed, with a maximum tensile strength up to 3 MPa (without boron), much lower strengths. Measurements at lower sintering temperatures were not feasible, because they delaminated during clamping in the testing machine. Actually, a higher tensile strength was expected, due to the larger contact area between both materials.
A possible reason for this result can be assumed comparing the interface of the composites with dense metallic layers and porous metallic layers. Both show mixed oxide phase, while the only visible difference is, that the composites with the dense metallic layer have an interface with a lower roughness and less micro undercuts. Hence, the authors assume that especially the micro undercuts give strength and not the phases. So regarding design, undercuts or a materials gradient should be included in the composite. However, these results shall be proven in further investigations.
The presented work shows co-sintering results of metal-ceramic symmetric and asymmetric composites. The investigations exhibited that a mismatch in sintering behaviour due to a less shrinking metallic layer, led to a reduced density of the zirconia layer in comparison to a free sintered zirconia layer after sintering. Furthermore, mismatches in the strain rate cause cracks in the ceramic layer.
On the other hand, adapting of sintering behaviour allows manufacturing of defect-free metal-ceramic composites with dense ceramic layers. Largest dimensions of manufactured composites were 10 cm×10 cm. X-ray diffraction measurements exhibited that there was no stress induced transformation from the tetragonal to the monoclinic phase due to mismatches in the CTE.
Adhesive tensile strength measurements showed a strong dependence of strength in terms of sintering temperature and boron content while maximum measured strength was 10.8 MPa.
This project was funded by the German Ministry of Economic Affairs and Energy (BMWi) through the German Federation of Industrial Research Associations (“Arbeitsgemeinschaft industrieller Forschungsvereinigung-AiF”) under the IGF-project number 18520 BR.
The authors declare no conflicts ofinterest regarding this paper.
[1] |
Knowles TP, Vendruscolo M, Dobson CM (2014) The amyloid state and its association with protein misfolding diseases. Nat Rev Mol Cell Biol 15: 384–396. doi: 10.1038/nrm3810
![]() |
[2] |
Hardy JA, Higgins GA (1992) Alzheimers disease-the amyloid cascade hyopothesis. Science 256: 184–185. doi: 10.1126/science.1566067
![]() |
[3] |
Arriagada PV, Growdon JH, Hedleywhyte ET, et al. (1992) Neurofibrillary tangles but not senile plaques parellel duration and severity of Alzheimers disease. Neurology 42: 631–639. doi: 10.1212/WNL.42.3.631
![]() |
[4] |
Terry RD, Masliah E, Salmon DP, et al. (1991) Physical basis of cognitve alterations in Alzheimers disease-synapse loss is the major correlate of cognitive impairment. Ann Neurol 30: 572–580. doi: 10.1002/ana.410300410
![]() |
[5] |
Viola KL, Sbarboro J, Sureka R, et al. (2015) Towards non-invasive diagnostic imaging of early-stage Alzheimer's disease. Nat Nanotechnol 10: 91–98. doi: 10.1038/nnano.2014.254
![]() |
[6] | Hyman B, Tanzi R (1992) Amyloid, dementia and Alzheimer's disease. Curr Opin Neurol Neurosur 5: 88–93. |
[7] |
Cummings BJ, Pike CJ, Shankle R, et al. (1996) b-Amyloid deposition and other measures of neuropathology predict cognitive status in Alzheimer's disease. Neurobiol Aging 17: 921–933. doi: 10.1016/S0197-4580(96)00170-4
![]() |
[8] |
Cummings JL, Morstorf T, Zhong K (2014) Alzheimer's disease drug-development pipeline: Few candidates, frequent failures. Alzheimers Res Ther 6: 37. doi: 10.1186/alzrt269
![]() |
[9] |
Goure WF, Krafft GA, Jerecic J, et al. (2014) Targeting the proper amyloid-β neuronal toxins: A path forward for Alzheimer's disease immunotherapeutics. Alzheimers Res Ther 6: 42. doi: 10.1186/alzrt272
![]() |
[10] |
Karran E, Hardy J (2014) A critique of the drug discovery and phase 3 clinical programs targeting the amyloid hypothesis for Alzheimer disease. Ann Neurol 76: 185–205. doi: 10.1002/ana.24188
![]() |
[11] |
Karran E, Hardy J (2014) Antiamyloid therapy for Alzheimer's disease-are we on the right road? New Engl J Med 370: 377–378. doi: 10.1056/NEJMe1313943
![]() |
[12] |
Frackowiak J, Zoltowska A, Wisniewski HM (1994) Nonfibrillar β-amyloid protein is associated with smooth-muscle cells of vessel walls in Alzheimer disease. J Neuropath Exp Neur 53: 637–645. doi: 10.1097/00005072-199411000-00011
![]() |
[13] |
Oda T, Pasinetti GM, Osterburg HH, et al. (1994) Purification and characterization of brain clusterin. Biochem Bioph Res Co 204: 1131–1136. doi: 10.1006/bbrc.1994.2580
![]() |
[14] |
Oda T, Wals P, Osterburg HH, et al. (1995) Clusterin (apoJ) alters the aggregation of amyloid β peptide (Aβ(1-42)) and forms slowly sedimenting Aβ complexes that cuase oxidative stress. Exp Neurol 136: 22–31. doi: 10.1006/exnr.1995.1080
![]() |
[15] |
Esparza TJ, Zhao H, Cirrito JR, et al. (2013) Amyloid-β oligomerization in Alzheimer dementia versus high-pathology controls. Ann Neurol 73: 104–119. doi: 10.1002/ana.23748
![]() |
[16] |
Gong YS, Chang L, Viola KL, et al. (2003) Alzheimer's disease-affected brain: Presence of oligomeric A β ligands (ADDLs) suggests a molecular basis for reversible memory loss. P Natl Acad Sci USA 100: 10417–10422. doi: 10.1073/pnas.1834302100
![]() |
[17] |
Kayed R, Head E, Thompson JL, et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300: 486–489. doi: 10.1126/science.1079469
![]() |
[18] |
Noguchi A, Matsumura S, Dezawa M, et al. (2009) Isolation and characterization of patient-derived, toxic, high mass amyloid β-protein (Aβ) assembly from Alzheimer disease brains. J Biol Chem 284: 32895–32905. doi: 10.1074/jbc.M109.000208
![]() |
[19] |
Pham E, Crews L, Ubhi K, et al. (2010) Progressive accumulation of amyloid-β oligomers in Alzheimer's disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins. FEBS J 277: 3051–3067. doi: 10.1111/j.1742-4658.2010.07719.x
![]() |
[20] | Gyure KA, Durham R, Stewart WF, et al. (2001) Intraneuronal Aβ-amyloid precedes development of amyloid plaques in Down syndrome. Arch Pathol Lab Med 125: 489–492. |
[21] |
Lacor PN, Buniel MC, Chang L, et al. (2004) Synaptic targeting by Alzheimer's-related amyloid β oligomers. J Neurosci 24: 10191–10200. doi: 10.1523/JNEUROSCI.3432-04.2004
![]() |
[22] |
Lesne SE, Sherman MA, Grant M, et al. (2013) Brain amyloid-β oligomers in ageing and Alzheimer's disease. Brain 136: 1383–1398. doi: 10.1093/brain/awt062
![]() |
[23] |
Georganopoulou DG, Chang L, Nam JM, et al. (2005) Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer's disease. P Natl Acad Sci USA 102: 2273–2276. doi: 10.1073/pnas.0409336102
![]() |
[24] |
Bruggink KA, Jongbloed W, Biemans EALM, et al. (2013) Amyloid-β oligomer detection by ELISA in cerebrospinal fluid and brain tissue. Anal Biochem 433: 112–120. doi: 10.1016/j.ab.2012.09.014
![]() |
[25] |
Englund H, Gunnarsson MD, Brundin RM, et al. (2009) Oligomerization partially explains the lowering of Aβ42 in Alzheimer's disease cerebrospinal fluid. Neurodegener Dis 6: 139–147. doi: 10.1159/000225376
![]() |
[26] |
Fukumoto H, Tokuda T, Kasai T, et al. (2010) High-molecular-weight β-amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients. FASEB J 24: 2716–2726. doi: 10.1096/fj.09-150359
![]() |
[27] |
Gao CM, Yam AY, Wang X, et al. (2010) Aβ40 Oligomers identified as a potential biomarker for the diagnosis of Alzheimer's disease. PLoS One 5: e15725. doi: 10.1371/journal.pone.0015725
![]() |
[28] |
Herskovits AZ, Locascio JJ, Peskind ER, et al. (2013) A luminex assay detects amyloid-β oligomers in Alzheimer's disease cerebrospinal fluid. PLoS One 8: e67898. doi: 10.1371/journal.pone.0067898
![]() |
[29] |
Holtta M, Hansson O, Andreasson U, et al. (2013) Evaluating amyloid-β oligomers in cerebrospinal fluid as a biomarker for Alzheimer's disease. PLoS One 8: e66381. doi: 10.1371/journal.pone.0066381
![]() |
[30] |
Jongbloed W, Bruggink KA, Kester MI, et al. (2015) Amyloid-β oligomers relate to cognitive decline in Alzheimer's disease. J Alzheimers Dis 45: 35–43. doi: 10.3233/JAD-142136
![]() |
[31] |
Santos AN, Ewers M, Minthon L, et al. (2012) Amyloid-β oligomers in cerebrospinal fluid are associated with cognitive decline in patients with Alzheimer's disease. J Alzheimers Dis 29: 171–176. doi: 10.3233/JAD-2012-111361
![]() |
[32] |
Lesne S, Koh MT, Kotilinek L, et al. (2006) A specific amyloid-β protein assembly in the brain impairs memory. Nature 440: 352–357. doi: 10.1038/nature04533
![]() |
[33] |
Ono K, Condron MM, Teplow DB (2009) Structure-neurotoxicity relationships of amyloid β-protein oligomers. P Natl Acad Sci USA 106: 14745–14750. doi: 10.1073/pnas.0905127106
![]() |
[34] |
Quist A, Doudevski L, Lin H, et al. (2005) Amyloid ion channels: A common structural link for protein-misfolding disease. P Natl Acad Sci USA 102: 10427–10432. doi: 10.1073/pnas.0502066102
![]() |
[35] |
Shankar GM, Bloodgood BL, Townsend M, et al. (2007) Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J Neurosci 27: 2866–2875. doi: 10.1523/JNEUROSCI.4970-06.2007
![]() |
[36] |
Shankar GM, Li S, Mehta TH, et al. (2008) Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 14: 837–842. doi: 10.1038/nm1782
![]() |
[37] |
Townsend M, Shankar GM, Mehta T, et al. (2006) Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: A potent role for trimers. J Physiol 572: 477–492. doi: 10.1113/jphysiol.2005.103754
![]() |
[38] |
Lambert MP, Barlow AK, Chromy BA, et al. (1998) Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. P Natl Acad Sci USA 95: 6448–6453. doi: 10.1073/pnas.95.11.6448
![]() |
[39] |
Walsh DM, Klyubin I, Fadeeva JV, et al. (2002) Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416: 535–539. doi: 10.1038/416535a
![]() |
[40] |
Zhao J, Li A, Rajsombath M, et al. (2018) Soluble Aβ Oligomers Impair Dipolar Heterodendritic Plasticity by Activation of mGluR in the Hippocampal CA1 Region. iScience 6: 138–150. doi: 10.1016/j.isci.2018.07.018
![]() |
[41] |
De Felice FG, Wu D, Lambert MP, et al. (2008) Alzheimer's disease-type neuronal tau hyperphosphorylation induced by Aβ oligomers. Neurobiol Aging 29: 1334–1347. doi: 10.1016/j.neurobiolaging.2007.02.029
![]() |
[42] |
Ma QL, Yang F, Rosario ER, et al. (2009) β-amyloid oligomers induce phosphorylation of tau and inactivation of insulin receptor substrate via c-Jun N-terminal kinase signaling: Suppression by omega-3 fatty acids and curcumin. J Neurosci 29: 9078–9089. doi: 10.1523/JNEUROSCI.1071-09.2009
![]() |
[43] |
Resende R, Ferreiro E, Pereira C, et al. (2008) ER stress is involved in Aβ-induced GSK-3β activation and tau phosphorylation. J Neurosci Res 86: 2091–2099. doi: 10.1002/jnr.21648
![]() |
[44] |
Tomiyama T, Matsuyama S, Iso H, et al. (2010) A mouse model of amyloid-β oligomers: their contribution to synaptic alteration, abnormal tau phosphorylation, glial activation, and neuronal loss in vivo. J Neurosci 30: 4845–4856. doi: 10.1523/JNEUROSCI.5825-09.2010
![]() |
[45] |
Zempel H, Thies E, Mandelkow E, et al. (2010) A Oligomers Cause Localized Ca2+ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines. J Neurosci 30: 11938–11950. doi: 10.1523/JNEUROSCI.2357-10.2010
![]() |
[46] |
Heinitz K, Beck M, Schliebs R, et al. (2006) Toxicity mediated by soluble oligomers of β-amyloid(1‑42) on cholinergic SN56.B5.G4 cells. J Neurochem 98: 1930–1945. doi: 10.1111/j.1471-4159.2006.04015.x
![]() |
[47] |
Nunes-Tavares N, Santos LE, Stutz B, et al. (2012) Inhibition of choline acetyltransferase as a mechanism for cholinergic dysfunction induced by amyloid-β peptide oligomers. J Biol Chem 287: 19377–19385. doi: 10.1074/jbc.M111.321448
![]() |
[48] |
De Felice FG, Velasco PT, Lambert MP, et al. (2007) Aβ oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem 282: 11590–11601. doi: 10.1074/jbc.M607483200
![]() |
[49] | Longo VD, Viola KL, Klein WL, et al. (2000) Reversible inactivation of superoxide-sensitive aconitase in Aβ1-42-treated neuronal cell lines. J Neurochem 75: 1977–1985. |
[50] |
Sponne I, Fifre A, Drouet B, et al. (2003) Apoptotic neuronal cell death induced by the non-fibrillar amyloid-β peptide proceeds through an early reactive oxygen species-dependent cytoskeleton perturbation. J Biol Chem 278: 3437–3445. doi: 10.1074/jbc.M206745200
![]() |
[51] |
Tabner BJ, El-Agnaf OMA, Turnbull S, et al. (2005) Hydrogen peroxide is generated during the very early stages of aggregation of the amyloid peptides implicated in Alzheimer disease and familial British dementia. J Biol Chem 280: 35789–35792. doi: 10.1074/jbc.C500238200
![]() |
[52] |
Alberdi E, Wyssenbach A, Alberdi M, et al. (2013) Ca2+-dependent endoplasmic reticulum stress correlates with astrogliosis in oligomeric amyloid β-treated astrocytes and in a model of Alzheimer's disease. Aging Cell 12: 292–302. doi: 10.1111/acel.12054
![]() |
[53] |
Nishitsuji K, Tomiyama T, Ishibashi K, et al. (2009) The E693Δ mutation in amyloid precursor protein increases intracellular accumulation of amyloid β oligomers and causes endoplasmic reticulum stress-induced apoptosis in cultured cells. Am J Pathol 174: 957–969. doi: 10.2353/ajpath.2009.080480
![]() |
[54] |
Lacor PN, Buniel MC, Furlow PW, et al. (2007) Aβ oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J Neurosci 27: 796–807. doi: 10.1523/JNEUROSCI.3501-06.2007
![]() |
[55] |
Roselli F (2005) Soluble β-Amyloid1-40 induces NMDA-dependent degradation of postsynaptic density-95 at glutamatergic synapses. J Neurosci 25: 11061–11070. doi: 10.1523/JNEUROSCI.3034-05.2005
![]() |
[56] |
Snyder EM, Nong Y, Almeida CG, et al. (2005) Regulation of NMDA receptor trafficking by amyloid-β. Nat Neurosci 8: 1051–1058. doi: 10.1038/nn1503
![]() |
[57] | Zhao WQ, De Felice FG, Fernandez S, et al. (2007) Amyloid β oligomers induce impairment of neuronal insulin receptors. FASEB J 22: 246–260. |
[58] |
De Felice FG, Vieira MN, Bomfim TR, et al. (2009) Protection of synapses against Alzheimer's-linked toxins: insulin signaling prevents the pathogenic binding of Aβ oligomers. Proc Natl Acad Sci USA 106: 1971–1976. doi: 10.1073/pnas.0809158106
![]() |
[59] |
Koffie RM, Meyer-Luehmann M, Hashimoto T, et al. (2009) Oligomeric amyloid-β associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques. P Natl Acad Sci USA 106: 4012–4017. doi: 10.1073/pnas.0811698106
![]() |
[60] |
Decker H, Lo KY, Unger SM, et al. (2010) Amyloid-Peptide oligomers disrupt axonal transport through an NMDA receptor-dependent mechanism that is mediated by glycogen synthase kinase 3 in primary cultured hippocampal neurons. J Neurosci 30: 9166–9171. doi: 10.1523/JNEUROSCI.1074-10.2010
![]() |
[61] |
Pigino G, Morfini G, Atagi Y, et al. (2009) Disruption of fast axonal transport is a pathogenic mechanism for intraneuronal amyloid β. P Natl Acad Sci USA 106: 5907–5912. doi: 10.1073/pnas.0901229106
![]() |
[62] |
Poon WW, Blurton-Jones M, Tu CH, et al. (2011) β-Amyloid impairs axonal BDNF retrograde trafficking. Neurobiol Aging 32: 821–833. doi: 10.1016/j.neurobiolaging.2009.05.012
![]() |
[63] |
Hu J, Akama KT, Krafft GA, et al. (1998) Amyloid-β peptide activates cultured astrocytes: Morphological alterations, cytokine induction and nitric oxide release. Brain Res 785: 195–206. doi: 10.1016/S0006-8993(97)01318-8
![]() |
[64] |
Jimenez S, Baglietto-Vargas D, Caballero C, et al. (2008) Inflammatory response in the hippocampus of PS1M146L/APP751SL mouse model of Alzheimer's disease: Age-dependent switch in the microglial phenotype from alternative to classic. J Neurosci 28: 11650–11661. doi: 10.1523/JNEUROSCI.3024-08.2008
![]() |
[65] |
Bhaskar K, Miller M, Chludzinski A, et al. (2009) The PI3K-Akt-mTOR pathway regulates a oligomer induced neuronal cell cycle events. Mol Neurodegener 4: 1–18. doi: 10.1186/1750-1326-4-1
![]() |
[66] |
Varvel NH, Bhaskar K, Patil AR, et al. (2008) Aβ oligomers induce neuronal cell cycle events in Alzheimer's disease. J Neurosci 28: 10786–10793. doi: 10.1523/JNEUROSCI.2441-08.2008
![]() |
[67] |
Kim HJ, Chae SC, Lee DK, et al. (2003) Selective neuronal degeneration induced by soluble oligomeric amyloid β protein. FASEB J 17: 118–120. doi: 10.1096/fj.01-0987fje
![]() |
[68] |
Roher AE, Lowenson JD, Clarke S, et al. (1993) β-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. P Natl Acad Sci USA 90: 10836. doi: 10.1073/pnas.90.22.10836
![]() |
[69] |
Näslund J, Schierhorn A, Hellman U, et al. (1994) Relative abundance of Alzheimer Aβ amyloid peptide variants in Alzheimer disease and normal aging. P Natl Acad Sci USA 91: 8378. doi: 10.1073/pnas.91.18.8378
![]() |
[70] |
Vandersteen A, Hubin E, Sarroukh R, et al. (2012) A comparative analysis of the aggregation behavior of amyloid-β peptide variants. FEBS Lett 586: 4088–4093. doi: 10.1016/j.febslet.2012.10.022
![]() |
[71] |
Barrow CJ, Yasuda A, Kenny PTM, et al. (1992) Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease: Analysis of circular dichroism spectra. J Mol Biol 225: 1075–1093. doi: 10.1016/0022-2836(92)90106-T
![]() |
[72] |
Barrow CJ, Zagorski MG (1991) Solution structures of β peptide and its constituent fragments: Relation to amyloid deposition. Science 253: 179–182. doi: 10.1126/science.1853202
![]() |
[73] |
Inouye H, Fraser PE, Kirschner DA (1993) Structure of β-crystallite assemblies formed by Alzheimer β-amyloid protein analogs-analysis by x-ray diffraction. Biophys J 64: 502–519. doi: 10.1016/S0006-3495(93)81393-6
![]() |
[74] |
Torok M, Milton S, Kayed R, et al. (2002) Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling. J Biol Chem 277: 40810–40815. doi: 10.1074/jbc.M205659200
![]() |
[75] |
Antzutkin ON, Balbach JJ, Leapman RD, et al. (2000) Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils. P Natl Acad Sci USA 97: 13045–13050. doi: 10.1073/pnas.230315097
![]() |
[76] |
Petkova AT, Leapman RD, Guo ZH, et al. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science 307: 262–265. doi: 10.1126/science.1105850
![]() |
[77] |
Tycko R (2006) Solid-state NMR as a probe of amyloid structure. Protein Peptide Lett 13: 229–234. doi: 10.2174/092986606775338470
![]() |
[78] |
Pastor MT, Kuemmerer N, Schubert V, et al. (2008) Amyloid toxicity is independent of polypeptide sequence, length and chirality. J Mol Biol 375: 695–707. doi: 10.1016/j.jmb.2007.08.012
![]() |
[79] |
Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333–366. doi: 10.1146/annurev.biochem.75.101304.123901
![]() |
[80] |
Xue WF, Homans SW, Radford SE (2008) Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci USA 105: 8926–8931. doi: 10.1073/pnas.0711664105
![]() |
[81] |
Murphy R (2007) Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins. BBA-Biomembranes 1768: 1923–1934. doi: 10.1016/j.bbamem.2006.12.014
![]() |
[82] |
Ghosh P, Vaidya A, Kumar A, et al. (2016) Determination of critical nucleation number for a single nucleation amyloid-β aggregation model. Math Biosci 273: 70–79. doi: 10.1016/j.mbs.2015.12.004
![]() |
[83] |
Garai K, Sahoo B, Sengupta P, et al. (2008) Quasihomogeneous nucleation of amyloid β yields numerical bounds for the critical radius, the surface tension, and the free energy barrier for nucleus formation. J Chem Phys 128: 045102. doi: 10.1063/1.2822322
![]() |
[84] |
Novo M, Freire S, Al-Soufi W (2018) Critical aggregation concentration for the formation of early Amyloid-β(1-42) oligomers. Sci Rep 8: 1783. doi: 10.1038/s41598-018-19961-3
![]() |
[85] |
Xue C, Lin TY, Chang D, et al. (2017) Thioflavin T as an amyloid dye: Fibril quantification, optimal concentration and effect on aggregation. Roy Soc Open Sci 4: 160696. doi: 10.1098/rsos.160696
![]() |
[86] |
Kodali R, Wetzel R (2007) Polymorphism in the intermediates and products of amyloid assembly. Curr Opin Struc Biol 17: 48–57. doi: 10.1016/j.sbi.2007.01.007
![]() |
[87] |
Kodali R, Williams AD, Chemuru S, et al. (2010) Aβ(1-40) forms five distinct amyloid structures whose β-sheet contents and fibril stabilities are correlated. J Mol Biol 401: 503–517. doi: 10.1016/j.jmb.2010.06.023
![]() |
[88] |
Meinhardt J, Sachse C, Hortschansky P, et al. (2009) Aβ(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. J Mol Biol 386: 869–877. doi: 10.1016/j.jmb.2008.11.005
![]() |
[89] |
Tycko R (2015) Amyloid polymorphism: Structural basis and neurobiological relevance. Neuron 86: 632–645. doi: 10.1016/j.neuron.2015.03.017
![]() |
[90] |
Colletier JP, Laganowsky A, Landau M, et al. (2011) Molecular basis for amyloid-β polymorphism. P Natl Acad Sci USA 108: 16938–16943. doi: 10.1073/pnas.1112600108
![]() |
[91] |
Crowther RA, Goedert M (2000) Abnormal Tau-containing filaments in Neurodegenerative Disease. J Struct Biol 130: 271–279. doi: 10.1006/jsbi.2000.4270
![]() |
[92] |
Lu JX, Qiang W, Yau WM, et al. (2013) Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue. Cell 154: 1257–1268. doi: 10.1016/j.cell.2013.08.035
![]() |
[93] |
Qiang W, Yau WM, Lu JX, et al. (2017) Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes. Nature 541: 217–221. doi: 10.1038/nature20814
![]() |
[94] |
Paravastu AK, Qahwash I, Leapman RD, et al. (2009) Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure. P Natl Acad Sci USA 106: 7443–7448. doi: 10.1073/pnas.0812033106
![]() |
[95] |
Yates EA, Legleiter J (2014) Preparation protocols of Aβ(1-40) promote the formation of polymorphic aggregates and altered interactions with lipid bilayers. Biochemistry 53: 7038–7050. doi: 10.1021/bi500792f
![]() |
[96] |
Teplow DB (2013) On the subject of rigor in the study of amyloid β-protein assembly. Alzheimers Res Ther 5: 39. doi: 10.1186/alzrt203
![]() |
[97] |
Lee MC, Yu WC, Shih YH, et al. (2018) Zinc ion rapidly induces toxic, off-pathway amyloid-β oligomers distinct from amyloid-β derived diffusible ligands in Alzheimer's disease. Sci Rep 8: 1–16. doi: 10.1038/s41598-017-17765-5
![]() |
[98] |
Ryan DA, Narrow WC, Federoff HJ, et al. (2010) An improved method for generating consistent soluble amyloid-β oligomer preparations for in vitro neurotoxicity studies. J Neurosci Meth 190: 171–179. doi: 10.1016/j.jneumeth.2010.05.001
![]() |
[99] |
Barghorn S, Nimmrich V, Striebinger A, et al. (2005) Globular amyloid β-peptide1-42 oligomer-A homogenous and stable neuropathological protein in Alzheimer's disease. J Neurochem 95: 834–847. doi: 10.1111/j.1471-4159.2005.03407.x
![]() |
[100] |
Thibaudeau TA, Anderson RT, Smith DM (2018) A common mechanism of proteasome impairment by neurodegenerative disease-associated oligomers. Nat Commun 9: 1097. doi: 10.1038/s41467-018-03509-0
![]() |
[101] |
Stine WB, Dahlgren KN, Krafft GA, et al. (2003) In vitro characterization of conditions for amyloid-b peptide oligomerization and fibrillogenesis. J Biol Chem 278: 11612–11622. doi: 10.1074/jbc.M210207200
![]() |
[102] | Stine WB, Jungbauer L, Yu C, et al. (2011) Preparing synthetic Aβ in different aggregation states, In: Roberson ED (editor.), Alzheimer's Disease and Frontotemporal Dementia. Methods in Molecular Biology (Methods and Protocols), Totowa, NJ: Humana Press, 13–32. |
[103] | Benninger RJ, David T (1983) An improved method of preparing the amyloid β-protein for fibrillogenesis and neurotoxicity experiments. Brain Res Rev 287: 173–196. |
[104] |
Ryan TM, Caine J, Mertens HDT, et al. (2013) Ammonium hydroxide treatment of Aβ produces an aggregate free solution suitable for biophysical and cell culture characterization. PeerJ 1: e73. doi: 10.7717/peerj.73
![]() |
[105] |
Bitan G, Lomakin A, Teplow DB (2001) Amyloid β-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J Biol Chem 276: 35176–35184. doi: 10.1074/jbc.M102223200
![]() |
[106] | Lesne SE (2013) Breaking the code of amyloid-β oligomers. Int J Cell Biol 2013: 950783. |
[107] |
Sengupta U, Nilson AN, Kayed R (2016) The role of amyloid-β oligomers in toxicity, propagation, and immunotherapy. EBioMedicine 6: 42–49. doi: 10.1016/j.ebiom.2016.03.035
![]() |
[108] |
Benilova I, Karran E, De Strooper B (2012) The toxic Aβ oligomer and Alzheimer's disease: An emperor in need of clothes. Nat Neurosci 15: 349–357. doi: 10.1038/nn.3028
![]() |
[109] | Ferreira ST, Lourenco MV, Oliveira MM, et al. (2015) Soluble amyloid-β oligomers as synaptotoxins leading to cognitive impairment in Alzheimer's disease. Front Cell Neurosci 9: 191. |
[110] |
Cline EN, Bicca MA, Viola KL, et al. (2018) The amyloid-β oligomer hypothesis: Beginning of the third decade. J Alzheimers Dis 64: S567–S610. doi: 10.3233/JAD-179941
![]() |
[111] |
Brody DL, Jiang H, Wildburger N, et al. (2017) Non-canonical soluble amyloid-β aggregates and plaque buffering: Controversies and future directions for target discovery in Alzheimer's disease. Alzheimers Res Ther 9: 62. doi: 10.1186/s13195-017-0293-3
![]() |
[112] |
Sherman MA, LaCroix M, Amar F, et al. (2016) Soluble conformers of Aβ and Tau alter selective proteins governing axonal transport. J Neurosci 36: 9647–9658. doi: 10.1523/JNEUROSCI.1899-16.2016
![]() |
[113] |
O'Malley TT, Oktaviani NA, Zhang D, et al. (2014) Aβ dimers differ from monomers in structural propensity, aggregation paths and population of synaptotoxic assemblies. Biochem J 461: 413–426. doi: 10.1042/BJ20140219
![]() |
[114] |
Cheng IH, Scearce-Levie K, Legleiter J, et al. (2007) Accelerating amyloid-β fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models. J Biol Chem 282: 23818–23828. doi: 10.1074/jbc.M701078200
![]() |
[115] |
Amar F, Sherman MA, Rush T, et al. (2017) The amyloid-β oligomer Aβ*56 induces specific alterations in neuronal signaling that lead to tau phosphorylation and aggregation. Sci Signal 10: eaal2021. doi: 10.1126/scisignal.aal2021
![]() |
[116] |
Liu P, Reed MN, Kotilinek LA, et al. (2015) Quaternary structure defines a large class of amyloid-β oligomers neutralized by sequestration. Cell Rep 11: 1760–1771. doi: 10.1016/j.celrep.2015.05.021
![]() |
[117] |
Knight EM, Kim SH, Kottwitz JC, et al. (2016) Effective anti-Alzheimer Aβ therapy involves depletion of specific Aβ oligomer subtypes. Neurol Neuroimmunol Neuroinflamm 3: e237. doi: 10.1212/NXI.0000000000000237
![]() |
[118] |
Velasco PT, Heffern MC, Sebollela A, et al. (2012) Synapse-binding subpopulations of Aβ oligomers sensitive to peptide assembly blockers and scFv antibodies. ACS Chem Neurosci 3: 972–981. doi: 10.1021/cn300122k
![]() |
[119] |
Ryan TM, Roberts BR, McColl G, et al. (2015) Stabilization of nontoxic Aβ-oligomers: Insights into the mechanism of action of hydroxyquinolines in Alzheimer's disease. J Neurosci 35: 2871–2884. doi: 10.1523/JNEUROSCI.2912-14.2015
![]() |
[120] |
Ferreira IL, Ferreiro E, Schmidt J, et al. (2015) Aβ and NMDAR activation cause mitochondrial dysfunction involving ER calcium release. Neurobiol Aging 36: 680–692. doi: 10.1016/j.neurobiolaging.2014.09.006
![]() |
[121] |
Barz B, Liao Q, Strodel B (2018) Pathways of amyloid-β aggregation depend on oligomer shape. J Am Chem Soc 140: 319–327. doi: 10.1021/jacs.7b10343
![]() |
[122] |
Brito-Moreira J, Lourenco MV, Oliveira MM, et al. (2017) Interaction of amyloid-β (Aβ) oligomers with neurexin 2 and neuroligin 1 mediates synapse damage and memory loss in mice. J Biol Chem 292: 7327–7337. doi: 10.1074/jbc.M116.761189
![]() |
[123] |
Figueiredo CP, Clarke JR, Ledo JH, et al. (2013) Memantine rescues transient cognitive impairment caused by high-molecular-weight Aβ oligomers but not the persistent impairment induced by low-molecular-weight oligomers. J Neurosci 33: 9626–9317. doi: 10.1523/JNEUROSCI.0482-13.2013
![]() |
[124] |
Upadhaya AR, Lungrin I, Yamaguchi H, et al. (2012) High-molecular weight Aβ oligomers and protofibrils are the predominant Aβ species in the native soluble protein fraction of the AD brain. J Cell Mol Med 16: 287–295. doi: 10.1111/j.1582-4934.2011.01306.x
![]() |
[125] |
Mc Donald JM, O'Malley TT, Liu W, et al. (2015) The aqueous phase of Alzheimer's disease brain contains assemblies built from similar to 4 and similar to 7 kDa Aβ species. Alzheimers Dement 11: 1286–1305. doi: 10.1016/j.jalz.2015.01.005
![]() |
[126] |
Savioz A, Giannakopoulos P, Herrmann FR, et al. (2016) A study of Aβ oligomers in the temporal cortex and cerebellum of patients with neuropathologically confirmed Alzheimer's disease compared to aged controls. Neurodegener Dis 16: 398–406. doi: 10.1159/000446283
![]() |
[127] |
Breydo L, Kurouski D, Rasool S, et al. (2016) Structural differences between amyloid β oligomers. Biochem Bioph Res Co 477: 700–705. doi: 10.1016/j.bbrc.2016.06.122
![]() |
[128] |
Watanabe-Nakayama T, Ono K, Itami M, et al. (2016) High-speed atomic force microscopy reveals structural dynamics of amyloid β(1-42) aggregates. P Natl Acad Sci USA 113: 5835–5840. doi: 10.1073/pnas.1524807113
![]() |
[129] |
Matsumura S, Shinoda K, Yamada M, et al. (2011) Two distinct amyloid β-protein (Aβ) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses. J Biol Chem 286: 11555–11562. doi: 10.1074/jbc.M110.181313
![]() |
[130] |
Miller Y, Ma B, Nussinov R (2010) Polymorphism in Alzheimer Aβ amyloid organization reflects conformational selection in a rugged energy landscape. Chem Rev 110: 4820–4838. doi: 10.1021/cr900377t
![]() |
[131] |
Bernstein SL, Dupuis NF, Lazo ND, et al. (2009) Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nat Chem 1: 326–331. doi: 10.1038/nchem.247
![]() |
[132] |
Economou NJ, Giammona MJ, Do TD, et al. (2016) Amyloid β-protein assembly and Alzheimer's disease: Dodecamers of Aβ42, but not of Aβ40, seed fibril formation. J Am Chem Soc 138: 1772–1775. doi: 10.1021/jacs.5b11913
![]() |
[133] |
Shamitko-Klingensmith N, Boyd JW, Legleiter J (2016) Microtubule modification influences cellular response to amyloid-β exposure. AIMS Biophysics 3: 261–285. doi: 10.3934/biophy.2016.2.261
![]() |
[134] |
Yates EA, Cucco EM, Legleiter J (2011) Point mutations in Aβ induce polymorphic aggregates at liquid/solid interfaces. ACS Chem Neurosci 2: 294–307. doi: 10.1021/cn200001k
![]() |
[135] |
Yates EA, Owens SL, Lynch MF, et al. (2013) Specific domains of Aβ facilitate aggregation on and association with lipid bilayers. J Mol Biol 425: 1915–1933. doi: 10.1016/j.jmb.2013.03.022
![]() |
[136] |
Glabe CG (2008) Structural classification of toxic amyloid oligomers. J Biol Chem 283: 29639–29643. doi: 10.1074/jbc.R800016200
![]() |
[137] |
Chromy BA, Nowak RJ, Lambert MP, et al. (2003) Self-assembly of Aβ(1-42) into globular neurotoxins. Biochemistry 42: 12749–12760. doi: 10.1021/bi030029q
![]() |
[138] |
Glabe CG (2006) Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. Neurobiol Aging 27: 570–575. doi: 10.1016/j.neurobiolaging.2005.04.017
![]() |
[139] |
Lee EB, Leng LZ, Zhang B, et al. (2006) Targeting amyloid-β peptide (Aβ) oligomers by passive immunization with a conformation-selective monoclonal antibody improves learning and memory in Aβ precursor protein (APP) transgenic mice. J Biol Chem 281: 4292–4299. doi: 10.1074/jbc.M511018200
![]() |
[140] |
Lambert MP, Velasco PT, Chang L, et al. (2007) Monoclonal antibodies that target pathological assemblies of Aβ. J Neurochem 100: 23–35. doi: 10.1111/j.1471-4159.2006.04157.x
![]() |
[141] |
Hayden EY, Conovaloff JL, Mason A, et al. (2017) Preparation of pure populations of covalently stabilized amyloid β-protein oligomers of specific sizes. Anal Biochem 518: 78–85. doi: 10.1016/j.ab.2016.10.026
![]() |
[142] |
Ono K, Li L, Takamura Y, et al. (2012) Phenolic compounds prevent amyloid β-protein oligomerization and synaptic dysfunction by site-specific binding. J Biol Chem 287: 14631–14643. doi: 10.1074/jbc.M111.325456
![]() |
[143] |
Bitan G, Kirkitadze MD, Lomakin A, et al. (2003) Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways. P Natl Acad Sci USA 100: 330–335. doi: 10.1073/pnas.222681699
![]() |
[144] |
Al-Hilaly YK, Williams TL, Stewart-Parker M, et al. (2013) A central role for dityrosine crosslinking of Amyloid-β in Alzheimer's disease. Acta Neuropathol Commun 1: 83. doi: 10.1186/2051-5960-1-83
![]() |
[145] | Bush AI (2013) The metal theory of Alzheimer's disease. J Alzheimers Dis 33: S277–S281. |
[146] |
Butterfield DA, Boyd-Kimball D (2018) Oxidative stress, amyloid-β peptide, and altered key molecular pathways in the pathogenesis and progression of Alzheimer's disease. J Alzheimers Dis 62: 1345–1367. doi: 10.3233/JAD-170543
![]() |
[147] |
Smith DP, Ciccotosto GD, Tew DJ, et al. (2007) Concentration dependent Cu2+ induced aggregation and dityrosine formation of the Alzheimer's disease amyloid-β peptide. Biochemistry 46: 2881–2891. doi: 10.1021/bi0620961
![]() |
[148] |
Ryan TM, Kirby N, Mertens HDT, et al. (2015) Small angle X-ray scattering analysis of Cu2+-induced oligomers of the Alzheimer's amyloid β peptide. Metallomics 7: 536–543. doi: 10.1039/C4MT00323C
![]() |
[149] |
Takano K, Endo S, Mukaiyama A, et al. (2006) Structure of amyloid β fragments in aqueous environments. FEBS J 273: 150–158. doi: 10.1111/j.1742-4658.2005.05051.x
![]() |
[150] |
Streltsov VA, Varghese JN, Masters CL, et al. (2011) Crystal structure of the amyloid-β p3 fragment provides a model for oligomer formation in Alzheimer's disease. J Neurosci 31: 1419–1426. doi: 10.1523/JNEUROSCI.4259-10.2011
![]() |
[151] |
Liu C, Sawaya MR, Cheng PN, et al. (2011) Characteristics of amyloid-related oligomers revealed by crystal structures of macrocyclic β-sheet mimics. J Am Chem Soc 133: 6736–6744. doi: 10.1021/ja200222n
![]() |
[152] |
Pham JD, Chim N, Goulding CW, et al. (2013) Structures of oligomers of a peptide from β-amyloid. J Am Chem Soc 135: 12460–12467. doi: 10.1021/ja4068854
![]() |
[153] |
Spencer RK, Li H, Nowick JS (2014) X-ray crystallographic structures of trimers and higher-order oligomeric sssemblies of a peptide derived from Aβ17–36. J Am Chem Soc 136: 5595–5598. doi: 10.1021/ja5017409
![]() |
[154] |
Bhatia R, Lin H, Lal R (2000) Fresh and nonfibrillar amyloid b protein(1-42) induces rapid cellular degeneration in aged human fibroblasts: Evidence for AbP-channel-mediated cellular toxicity. FASEB 14: 1233–1243. doi: 10.1096/fasebj.14.9.1233
![]() |
[155] |
Lin H, Bhatia R, Lal R (2001) Amyloid b protein forms ion channels: Implications for Alzheimer's disease pathophysiology. FASEB 15: 2433–2444. doi: 10.1096/fj.01-0377com
![]() |
[156] |
Lin H, Zhu YJ, Lal R (1999) Amyloid-b protein (1–40) forms calcium-permeable, Zn2+-sensitive channel in reconstituted lipid vesicles. Biochemistry 38: 11189–11196. doi: 10.1021/bi982997c
![]() |
[157] |
Rhee SK, Quist AP, Lal R (1998) Amyloid b protein-(1-42) forms calcium-permeable, Zn2+-sensitive channel. J Biol Chem 273: 13379–13382. doi: 10.1074/jbc.273.22.13379
![]() |
[158] |
Parbhu A, Lin H, Thimm J, et al. (2002) Imaging real-time aggregation of amyloid β protein (1-42) by atomic force microscopy. Peptides 23: 1265–1270. doi: 10.1016/S0196-9781(02)00061-X
![]() |
[159] | Legleiter J, (2011) Assessing Aβ aggregation state by atomic force microscopy, In: Roberson ED (editor.), Alzheimer's Disease and Frontotemporal Dementia: Methods and Protocols, 57–70. |
[160] |
Kowalewski T, Holtzman DM (1999) In situ atomic force microscopy study of Alzheimer's β-amyloid peptide on different substrates: New insights into mechanism of β-sheet formation. Proc Natl Acad Sci USA 96: 3688–3693. doi: 10.1073/pnas.96.7.3688
![]() |
[161] |
Hane F, Drolle E, Gaikwad R, et al. (2011) Amyloid-β aggregation on model lipid membranes: An atomic force microscopy study. J Alzheimers Dis 26: 485–494. doi: 10.3233/JAD-2011-102112
![]() |
[162] |
Legleiter J, Fryer JD, Holtzman DM, et al. (2011) The modulating effect of mechanical changes in lipid bilayers caused by apoE-containing lipoproteins on Aβ induced membrane disruption. ACS Chem Neurosci 2: 588–599. doi: 10.1021/cn2000475
![]() |
[163] |
Yip CM, Elton EA, Darabie AA, et al. (2001) Cholesterol, a modulator of membrane-associated Ab-fibrillogenesis and neurotoxicity. J Mol Biol 311: 723–734. doi: 10.1006/jmbi.2001.4881
![]() |
[164] |
Yip CM, McLaurin J (2001) Amyloid-b assembly: A critical step in fibrillogensis and membrane disruption. Biophys J 80: 1359–1371. doi: 10.1016/S0006-3495(01)76109-7
![]() |
[165] |
Pifer PM, Yates EA, Legleiter J (2011) Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers. PLoS One 6: e16248. doi: 10.1371/journal.pone.0016248
![]() |
[166] |
Burke KA, Yates EA, Legleiter J (2013) Amyloid-forming proteins alter the local mechanical properties of lipid membranes. Biochemistry 52: 808–817. doi: 10.1021/bi301070v
![]() |
[167] |
Hane F, Tran G, Attwood S, et al. (2013) Cu2+ affects amyloid-β (1-42) aggregation by increasing peptide-peptide binding forces. PLoS One 8: e59005. doi: 10.1371/journal.pone.0059005
![]() |
[168] |
Kim BH, Palermo NY, Lovas S, et al. (2011) Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions. Biochemistry 50: 5154–5162. doi: 10.1021/bi200147a
![]() |
[169] |
Banerjee S, Sun Z, Hayden EY, et al. (2017) Nanoscale dynamics of amyloid-β42 oligomers as revealed by high-speed atomic force microscopy. ACS Nano 11: 12202–12209. doi: 10.1021/acsnano.7b05434
![]() |
[170] |
Yang T, Li S, Xu H, et al. (2017) Large soluble oligomers of amyloid β-protein from Alzheimer brain are far less neuroactive than the smaller oligomers to which they dissociate. J Neurosci 37: 152–163. doi: 10.1523/JNEUROSCI.1698-16.2016
![]() |
[171] |
Ahmed M, Davis J, Aucoin D, et al. (2010) Structural conversion of neurotoxic amyloid-β(1-42) oligomers to fibrils. Nat Struct Mol Biol 17: 561–556. doi: 10.1038/nsmb.1799
![]() |
[172] |
Chimon S, Shaibat MA, Jones CR, et al. (2007) Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid. Nat Struct Mol Biol 14: 1157–1164. doi: 10.1038/nsmb1345
![]() |
[173] |
Stroud JC, Liu C, Teng PK, et al. (2012) Toxic fibrillar oligomers of amyloid-β have cross-β structure. P Natl Acad Sci USA 109: 7717–7722. doi: 10.1073/pnas.1203193109
![]() |
[174] |
Gu L, Liu C, Stroud JC, et al. (2014) Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers. J Biol Chem 289: 27300–27313. doi: 10.1074/jbc.M114.569004
![]() |
[175] |
Teoh CL, Su D, Sahu S, et al. (2015) Chemical fluorescent probe for detection of Aβ oligomers. J Am Chem Soc 137: 13503–13509. doi: 10.1021/jacs.5b06190
![]() |
[176] |
Jameson LP, Dzyuba SV (2013) Aza-BODIPY: Improved synthesis and interaction with soluble Aβ1-42 oligomers. Bioorg Med Chem Lett 23: 1732–1735. doi: 10.1016/j.bmcl.2013.01.065
![]() |
[177] |
Ono M, Watanabe H, Kimura H, et al. (2012) BODIPY-based molecular probe for imaging of cerebral β-amyloid plaques. ACS Chem Neurosci 3: 319–324. doi: 10.1021/cn3000058
![]() |
[178] |
Verwilst P, Kim HR, Seo J, et al. (2017) Rational design of in vivo Tau tangle-selective near-infrared fluorophores: expanding the BODIPY universe. J Am Chem Soc 139: 13393–13403. doi: 10.1021/jacs.7b05878
![]() |
1. | Divine Wanduku, On the almost sure convergence of a stochastic process in a class of nonlinear multi-population behavioral models for HIV/AIDS with delayed ART treatment, 2020, 0736-2994, 1, 10.1080/07362994.2020.1848593 | |
2. | Divine Wanduku, Finite- and multi-dimensional state representations and some fundamental asymptotic properties of a family of nonlinear multi-population models for HIV/AIDS with ART treatment and distributed delays, 2021, 0, 1937-1179, 0, 10.3934/dcdss.2021005 | |
3. | Mohammad Ghani, Dynamics of spatio-temporal HIV–AIDS model with the treatments of HAART and immunotherapy, 2024, 12, 2195-268X, 1366, 10.1007/s40435-023-01284-5 |
powder | water | binder | plasticizer | de-foamer | surfactant | |
TZ-3YS-E | 44.5 | 45.1 | 4.3 | 5.7 | 0.2 | 0.2 |
metal powder 1 | 43.3 | 35.7 | 4.3 | 6.5 | 0.1 | 0.1 |
metal powder 2 | 80.5 | 15.6 | 1.6 | 2 | 0.1 | 0.2 |
metal powder 3 | 65.3 | 28.1 | 3 | 3.3 | 0.1 | 0.2 |
metal powder 4 | 80.5 | 15.6 | 1.6 | 2 | 0.1 | 0.2 |
composite | green | 1400 °C | |
layer thickness/µm | layer thickness/µm | shrinkage/% | |
1 | 9.5 ± 1.4 | 18.1 | |
3 | 11.6 ± 1.0 | 8.5 ± 1.4 | 26.7 |
4 | 8.2 ± 1.2 | 29.3 |
powder | water | binder | plasticizer | de-foamer | surfactant | |
TZ-3YS-E | 44.5 | 45.1 | 4.3 | 5.7 | 0.2 | 0.2 |
metal powder 1 | 43.3 | 35.7 | 4.3 | 6.5 | 0.1 | 0.1 |
metal powder 2 | 80.5 | 15.6 | 1.6 | 2 | 0.1 | 0.2 |
metal powder 3 | 65.3 | 28.1 | 3 | 3.3 | 0.1 | 0.2 |
metal powder 4 | 80.5 | 15.6 | 1.6 | 2 | 0.1 | 0.2 |
composite | green | 1400 °C | |
layer thickness/µm | layer thickness/µm | shrinkage/% | |
1 | 9.5 ± 1.4 | 18.1 | |
3 | 11.6 ± 1.0 | 8.5 ± 1.4 | 26.7 |
4 | 8.2 ± 1.2 | 29.3 |