Salmon calcitonin: conformational changes and stabilizer effects

Shan-Yang Lin; Shan-Yang Lin

doi:10.3934/biophy.2015.4.695

AIMS Biophysics

2015, Volume 2, Issue 4: 695-723. doi: 10.3934/biophy.2015.4.695

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Review Topical Sections

Salmon calcitonin: conformational changes and stabilizer effects

Shan-Yang Lin ^,

Laboratory of Pharmaceutics & Biopharmaceutics, Department of Biotechnology and Pharmaceutical Technology, Yuanpei University, Hsin Chu 30015, Taiwan, ROC

Received: 03 October 2015 Accepted: 09 November 2015 Published: 11 November 2015

The therapeutic activity of peptides or protein drugs is highly dependent on their conformational structure. The protein structure is flexible and responds to external conditions, which may compromise the protein's native conformation and influence its physical and chemical stability. The physical and chemical stability of peptides or protein drugs are important characteristics of biopharmaceutical products. Calcitonin (CT) is a polypeptide hormone that participates in diverse physiological functions in humans; therefore, it is a potentially useful protein for investigations of different aspects of pharmacology and drug delivery systems. Of the different types of CT available for clinical use, salmon CT (sCT) is one of the most potent. In this review article, the commercially available sCT was selected as a suitable peptide candidate for the discussion of its stability and conformational changes in the aqueous and solid states using Fourier transform infrared (FTIR) spectroscopic analysis under different external conditions, including pH, temperature, drying method, and added excipients. Particularly, excipients that have been optimized as stabilizers of sCT in aqueous solution and as lyophilized and spray-dried drug formulations are also discussed.
- Salmon calcitonin,
- conformation,
- stability,
- solution,
- solid state,
- stabilizer
Citation: Shan-Yang Lin. Salmon calcitonin: conformational changes and stabilizer effects[J]. AIMS Biophysics, 2015, 2(4): 695-723. doi: 10.3934/biophy.2015.4.695

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Abstract

The therapeutic activity of peptides or protein drugs is highly dependent on their conformational structure. The protein structure is flexible and responds to external conditions, which may compromise the protein's native conformation and influence its physical and chemical stability. The physical and chemical stability of peptides or protein drugs are important characteristics of biopharmaceutical products. Calcitonin (CT) is a polypeptide hormone that participates in diverse physiological functions in humans; therefore, it is a potentially useful protein for investigations of different aspects of pharmacology and drug delivery systems. Of the different types of CT available for clinical use, salmon CT (sCT) is one of the most potent. In this review article, the commercially available sCT was selected as a suitable peptide candidate for the discussion of its stability and conformational changes in the aqueous and solid states using Fourier transform infrared (FTIR) spectroscopic analysis under different external conditions, including pH, temperature, drying method, and added excipients. Particularly, excipients that have been optimized as stabilizers of sCT in aqueous solution and as lyophilized and spray-dried drug formulations are also discussed.

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