Consequences of incorporating thiaproline and its oxidized derivatives into collagen triple helices.

ABSTRACT: (2R)-4-thiaproline (Thp) is an analog of proline, replacing C^γ in the pyrrolidine ring with sulfur. Its thiazolidine ring easily interconverts between endo and exo puckers due to a small energy barrier, which leads to destabilize polyproline helices. Collagen, composed of three polyproline II helices, mainly consists of X-Y-Gly triplets, where X is often proline and Y is frequently (2S,4R)-hydroxyproline. In this study, we incorporated Thp into either position-X or position-Y to investigate the consequences of such a replacement on the triple helix. Circular dichroism and differential scanning calorimetry analyses showed that the Thp-containing collagen-mimetic peptides (CMPs) can fold into stable triple helices, in which the substitution at position-Y exhibits a larger destabil

SUBMITTER: Hsu TL 

PROVIDER: S-EPMC10182727 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature