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

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

Volume: 15 Issue: 9

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

Affiliation:

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

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.

Cite this article as:

Zhao Jie, Huang Qi-Long, Tang Yue-Hua, Guo Zhan-Yun, Qiao Zhi-Song, Xu Gen-Jun and Feng You-Min, Equilibrium Folding of Porcine Insulin Precursor in the Presence of Redox Buffer: Implications for the Common Intermediates Shared by Its Unfolding/ Refolding Processes, Protein & Peptide Letters 2008; 15 (9) . https://dx.doi.org/10.2174/092986608785849227