Abstract
Sites of exendin-4 that that are relatively susceptible to degradation in plasma were identified with the aim of providing information for designing new exendin-4 analogues. The stability of exendin-4 in human plasma was evaluated in vitro. The results showed that the peptide was slowly degraded with a half-life of 9.57 h and the principal cleavage sites are between Thr5 and Phe6, Phe6 and Thr7, and Thr7 and Ser8 of the N-terminus region of exendin-4.
Keywords: Synthetic exendin-4, Glucagon-like peptide, Stability, Dipeptidyl peptidase-IV(DPP- V)
Protein & Peptide Letters
Title: Stability of Synthetic Exendin-4 in Human Plasma In Vitro
Volume: 14 Issue: 1
Author(s): Jie Chen, Ling Yu, Liping Wang, Xuexun Fang, Li Li and Wei Li
Affiliation:
Keywords: Synthetic exendin-4, Glucagon-like peptide, Stability, Dipeptidyl peptidase-IV(DPP- V)
Abstract: Sites of exendin-4 that that are relatively susceptible to degradation in plasma were identified with the aim of providing information for designing new exendin-4 analogues. The stability of exendin-4 in human plasma was evaluated in vitro. The results showed that the peptide was slowly degraded with a half-life of 9.57 h and the principal cleavage sites are between Thr5 and Phe6, Phe6 and Thr7, and Thr7 and Ser8 of the N-terminus region of exendin-4.
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Cite this article as:
Chen Jie, Yu Ling, Wang Liping, Fang Xuexun, Li Li and Li Wei, Stability of Synthetic Exendin-4 in Human Plasma In Vitro, Protein & Peptide Letters 2007; 14 (1) . https://dx.doi.org/10.2174/092986607779117272
DOI https://dx.doi.org/10.2174/092986607779117272 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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