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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Equilibrium Folding of Porcine Insulin Precursor in the Presence of Redox Buffer: Implications for the Common Intermediates Shared by Its Unfolding/ Refolding Processes

Author(s): Jie Zhao, Qi-Long Huang, Yue-Hua Tang, Zhan-Yun Guo, Zhi-Song Qiao, Gen-Jun Xu and You-Min Feng

Volume 15, Issue 9, 2008

Page: [972 - 979] Pages: 8

DOI: 10.2174/092986608785849227

Price: $65

Abstract

We use the procedure established for ‘disulfide stability analysis in redox system’ to investigate the unfolding process of porcine insulin precursor (PIP). Six major unfolding intermediates have been captured, in which four contain two disulfides, two contain one disulfide. Based on the characterization and analysis of the intermediates an unfolding pathway has been proposed, by which the native PIP unfolded through in turn 2SS and 1SS intermediates into fully reduced form. Besides, the comparison of the intermediates captured in PIP unfolding process with those intermediates captured in its refolding process revealed that some intermediates captured during both unfolding/refolding processes of PIP have identical disulfide pairing pattern, from which we suggest that the unfolding/refolding processes of PIP share some common intermediates but flow in the opposite direction.

Keywords: Insulin, single-chain insulin, folding, unfolding, intermediate, disulfide


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