Oxidative Folding of a Two-Chain Protein Having Three Interchain Disulfide Bonds. Synthesis of Bromelain Inhibitor VI Through Native Chain Assembly.

ABSTRACT: The recently renovated two-chain folding method, in which two native peptide chains without any sidechain protections and interchain scaffolds are just mixed in a buffer solution under optimized conditions, called native chain assembly (NCA), enabled efficient chemical synthesis of α-helix-rich insulin and its analogs, which are stabilized by two interchain disulfide (SS) bridges. Herein, this simple folding method has been successfully applied to the folding of a different-type two-chain protein, that is, bromelain inhibitor VI (BI-VI), which has abundant β-sheet structures and is stabilized by three interchain SS bridges. When the chemically synthesized native heavy (H)- and light (L)-chains of BI-VI were mixed at 4 °C in a pH of 10.0 buffer solution containing 2 mM GSH and 0.4 mM GSSG,

SUBMITTER: Iwaoka M 

PROVIDER: S-EPMC12223344 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature