Sequences of B-chain/domain 1-10/1-9 of insulin and insulin-like growth factor 1 determine their different folding behavior

Biochemistry
Yan ChenYou-Min Feng

Abstract

Although insulin and insulin-like growth factor-1 (IGF-1) belong to one family, insulin folds into one thermodynamically stable structure, while IGF-1-folds into two thermodynamically stable structures (native and swap forms). We have demonstrated previously that the bifurcating folding behavior of IGF-1 is mainly controlled by its B-domain. To further elucidate which parts of the sequences determine their different folding behavior, by exchanging the N-terminal sequences of mini-IGF-1 and recombinant porcine insulin precursor (PIP), we prepared four peptide models: [1-9]PIP, [1-10]mini-IGF-1, [1-4]PIP, and [1-5]mini-IGF-1 by means of protein engineering, and their disulfide rearrangement, V8 digestion, circular dichroic spectra, disulfide stability, and in vitro refolding were investigated. Among them only [1-9]PIP, like mini-IGF-1/IGF-1, was expressed in yeast as two isomers: isomer 1 (corresponding to swap IGF-1) and isomer 2 (corresponding to native IGF-1), which are supported by the experimental results of disulfide rearrangements, peptide mapping of V8 endoprotenase digests, circular dichroic analysis, in vitro refolding, and disulfide stability analysis. The other peptide models, [1-10]mini-IGF-1, [1-4]PIP, and [1-5]mini...Continue Reading

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Citations

Nov 17, 2007·Antioxidants & Redox Signaling·Zhan-Yun GuoYou-Min Feng
Aug 24, 2006·Bioscience, Biotechnology, and Biochemistry·Xi-Lian HuAn-Ju Zhang
Sep 20, 2018·Diabetes, Obesity & Metabolism·Ming LiuPeter Arvan
Jul 26, 2006·The Journal of Biological Chemistry·Qing-xin HuaMichael A Weiss
Apr 7, 2021·Molecular Metabolism·Balamurugan DhayalanMichael A Weiss
Oct 19, 2021·Frontiers in Endocrinology·Balamurugan DhayalanMichael A Weiss

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