ArticleChemistry (Weinheim an der Bergstrasse, Germany)2025
Oxidative Folding of a Two-Chain Protein Having Three Interchain Disulfide Bonds. Synthesis of Bromelain Inhibitor VI Through Native Chain Assembly.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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, native BI-VI was obtained surprisingly in a high isolated yield (53%) after 2 weeks. The obtained BI-VI showed complete inhibitory activity against bromelain, whereas each component chain exhibited essentially non-activity. The rate-limiting step of the two-chain folding was assumed to be the chain coupling between three-SS intermediates of the H-chain (3SS
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