Cysteine-based protein folding modulators for trapping intermediates and misfolded forms.

ABSTRACT: Folding is a key process to form functional conformations of proteins. Folding via on-pathway intermediates leads to the formation of native structures, while folding through off-pathways affords non-native and disease-causing forms. Trapping folding intermediates and misfolded forms is important for investigating folding mechanisms and disease-related biological properties of the misfolded proteins. We developed cysteine-containing dipeptides conjugated with amino acids possessing mono- and diamino-groups. In oxidative protein folding involving disulfide-bond formation, the addition of cysteine and oxidized glutathione readily promoted the folding to afford native forms. In contrast, despite the acceleration of disulfide-bond formation, non-native isomers formed in significantly in

SUBMITTER: Nishino H 

PROVIDER: S-EPMC9490518 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature