Topological Regulation of the Bioactive Conformation of a Disulfide-Rich Peptide, Heat-Stable Enterotoxin.

ABSTRACT: Heat-stable enterotoxin (ST_a) produced by enterotoxigenic E. coli causes acute diarrhea and also can be used as a specific probe for colorectal cancer cells. ST_a contains three intra-molecular disulfide bonds (C1-C4, C2-C5, and C3-C6 connectivity). The chemical synthesis of ST_a provided not only the native type of ST_a but also a topological isomer that had the native disulfide pairings. Interestingly, the activity of the topological isomer was approximately 1/10-1/2 that of the native ST_a. To further investigate the bioactive conformation of this molecule and the regulation of disulfide-coupled folding during its chemical syntheses, we examined the folding mechanism of ST_a that occurs during its chemical synthesis. Th

SUBMITTER: Shimamoto S 

PROVIDER: S-EPMC7587965 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature