Putative folding pathway of insulin-like growth factor-I

Archives of Biochemistry and Biophysics
R D RosenfeldT Arakawa

Abstract

Insulin-like growth factor-I (IGF-I) has three disulfide bonds and refolding of the fully reduced molecule generates varying ratios of correctly (PII) and incorrectly (PI) folded forms via several intermediates. All of the intermediates have the disulfide bond between Cys18 and 61 formed, indicating that formation of this disulfide is the first step in refolding. In order to further understand the refolding pathway, two intermediate froms, PIII with the additional disulfide Cys(6/47) formed and PIIIa with Cys(6/48) formed, were isolated. The oxidation of the remaining Cys48 and 52 in PIII and Cys47 and 52 in PIIIa would lead to PI and PII, respectively; however, air oxidation of these resulted in a rapid reshuffling into other intermediates as well as folding into the fully oxidized forms, and this occurred whether refolding was started with PIII or PIIIa. When oxidation occurred in the presence of an excess of oxidized glutathione, the predominant species generated were various glutathione adducts regardless of the initial intermediate form, indicating that formation of the last disulfide bond is not a favorable process relative to disulfide exchange when excess disulfides from oxidized glutathione are present. Interestingly, ...Continue Reading

Citations

Sep 24, 1999·The Biochemical Journal·Y YuanJ G Tang
Nov 17, 2007·Antioxidants & Redox Signaling·Zhan-Yun GuoYou-Min Feng
Jul 28, 1999·Protein Science : a Publication of the Protein Society·J Y ChangP H Lai
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Nov 9, 2002·Analytical Biochemistry·Jeannette WinterRainer Rudolph
May 20, 2017·Rapid Communications in Mass Spectrometry : RCM·Kenichiro FurukiHideto Yamaguchi
Oct 11, 2017·Current Protein & Peptide Science·Tsutomu Arakawa
Oct 11, 2017·Current Protein & Peptide Science·Tsutomu Arakawa
Nov 8, 2005·The Biochemical Journal·Jui-Yoa ChangPor-Hsiung Lai

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