Radioprotective effect of nanoceria and magnetic flower-like iron oxide microparticles on gamma radiation-induced damage in BSA protein

Mostean Bahreinipour; Hajar Zarei; Fariba Dashtestani; Jamal Rashidiani; Khadijeh Eskandari; Seyed Ali Moussavi Zarandi; Susan Kabudanian Ardestani; Hiroshi Watabe; Mostean Bahreinipour; Hajar Zarei; Fariba Dashtestani; Jamal Rashidiani; Khadijeh Eskandari; Seyed Ali Moussavi Zarandi; Susan Kabudanian Ardestani; Hiroshi Watabe

doi:10.3934/biophy.2021010

AIMS Biophysics

2021, Volume 8, Issue 2: 124-142. doi: 10.3934/biophy.2021010

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Radioprotective effect of nanoceria and magnetic flower-like iron oxide microparticles on gamma radiation-induced damage in BSA protein

Running title:Running Title: Radioprotective Effect of Nanostructures on BSA

1.
Department of Energy Engineering and Physics, Faculty of Physics, Amirkabir University of Technology, Tehran, Iran
2.
Persian Gulf Research Institute, Persian Gulf University Bushehr, Iran
3.
Cyclotron and Radioisotope Center (CYRIC), Tohoku University, Sendai, Miyagi, Japan
4.
Institute of Biochemistry & Biophysics, University of Tehran, Tehran, Iran
5.
Nanobiotechnology Research Center, Baqiyatallah University of Medical Science, Tehran, Iran

Received: 26 December 2020 Accepted: 04 March 2021 Published: 10 March 2021

Purpose
Gamma radiation at therapeutic doses can cause conformation changes in proteins and consequently damage cells/tissues associated with the initiation of several pathological disorders. In this study, serum albumin, the most abundant protein in plasma, was chosen as the protein sample.
Methods and Materials
Bovine serum albumin (BSA) was exposed to gamma radiation at a therapeutic dose (3 Gy) in the absence and presence of Ceria nanoparticles (CNPs) and flower-like Fe₃O₄ microparticles (FIOMPs). The conformational changes in BSA including primary, secondary, tertiary structures were then studied by UV-Vis, circular dichroism (CD), and fluorescence spectroscopy, respectively.
Results
The primary structure of gamma-irradiated BSA (IR-BSA) was conserved, whereas the secondary and tertiary structures were considerably changed. IR-BSA showed α-helix to β-sheet and random coil structure transition along with reduced fluorescence emission intensity compared to non-irradiated native BSA. Both CNPs and FIOMPs could inhibit the secondary and tertiary structural changes in IR-BSA by scavenging the reactive oxygen species produced during the radiolysis of water.
Conclusions
The radioprotective property of CNPs arises from enzyme mimetic activities (catalase, superoxide dismutase, and peroxidase) and their antioxidant capability against hydroxyl radicals. In case of FIOMPs, the radioprotective property is attributed to catalase mimetic activity (CAT), and a porous structure leading to increased ROS recombination with each other in the same radiolytic track, and subsequently decreased encounters with BSA. The latter mechanism of restricting ROS migration seems to be more dominant for FIOMPs. Both CNPs/FIOMPs themselves at low concentrations do not show a significant effect on the native protein conformation. These findings indicate that the proposed NPs/MPs can be good candidates for developing strong nano-radioprotectors.
- bovine serum albumin,
- gamma radiation,
- spectroscopy,
- ceria nanoparticles,
- flower microparticles,
- nano-radioprotector
Citation: Mostean Bahreinipour, Hajar Zarei, Fariba Dashtestani, Jamal Rashidiani, Khadijeh Eskandari, Seyed Ali Moussavi Zarandi, Susan Kabudanian Ardestani, Hiroshi Watabe. Radioprotective effect of nanoceria and magnetic flower-like iron oxide microparticles on gamma radiation-induced damage in BSA protein[J]. AIMS Biophysics, 2021, 8(2): 124-142. doi: 10.3934/biophy.2021010

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Abstract

Purpose

Gamma radiation at therapeutic doses can cause conformation changes in proteins and consequently damage cells/tissues associated with the initiation of several pathological disorders. In this study, serum albumin, the most abundant protein in plasma, was chosen as the protein sample.

Methods and Materials

Bovine serum albumin (BSA) was exposed to gamma radiation at a therapeutic dose (3 Gy) in the absence and presence of Ceria nanoparticles (CNPs) and flower-like Fe₃O₄ microparticles (FIOMPs). The conformational changes in BSA including primary, secondary, tertiary structures were then studied by UV-Vis, circular dichroism (CD), and fluorescence spectroscopy, respectively.

Results

The primary structure of gamma-irradiated BSA (IR-BSA) was conserved, whereas the secondary and tertiary structures were considerably changed. IR-BSA showed α-helix to β-sheet and random coil structure transition along with reduced fluorescence emission intensity compared to non-irradiated native BSA. Both CNPs and FIOMPs could inhibit the secondary and tertiary structural changes in IR-BSA by scavenging the reactive oxygen species produced during the radiolysis of water.

Conclusions

The radioprotective property of CNPs arises from enzyme mimetic activities (catalase, superoxide dismutase, and peroxidase) and their antioxidant capability against hydroxyl radicals. In case of FIOMPs, the radioprotective property is attributed to catalase mimetic activity (CAT), and a porous structure leading to increased ROS recombination with each other in the same radiolytic track, and subsequently decreased encounters with BSA. The latter mechanism of restricting ROS migration seems to be more dominant for FIOMPs. Both CNPs/FIOMPs themselves at low concentrations do not show a significant effect on the native protein conformation. These findings indicate that the proposed NPs/MPs can be good candidates for developing strong nano-radioprotectors.

Acknowledgments

This study was supported by Grants-in-Aid for Scientific Research No. 19H04296 from the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japanese Government. The authors gratefully acknowledge the use of the services, facilities, and the excellent experimental conditions provided by IBB, Baqiyatallah University of Medical Sciences (Tehran) and the Cyclotron and Radioisotope Center (CYRIC), Tohoku University, Japan.

Conflict of interest

All authors declare no conflicts of interest in this paper.

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