Peptoid Residues Make Diverse, Hyperstable Collagen Triple-Helices.

ABSTRACT: As the only ribosomally encoded N-substituted amino acid, proline promotes distinct secondary protein structures. The high proline content in collagen, the most abundant protein in the human body, is crucial to forming its hallmark structure: the triple-helix. For over five decades, proline has been considered compulsory for synthetic designs aimed at recapitulating collagen's structure and properties. Here we describe that N-substituted glycines (N-glys), also known as peptoid residues, exhibit a general triple-helical propensity similar to or greater than proline, enabling synthesis of stable triple-helical collagen mimetic peptides (CMPs) with unprecedented side chain diversity. Supported by atomic-resolution crystal structures as well as circular dichroism and computational characteriz

SUBMITTER: Kessler JL 

PROVIDER: S-EPMC9209468 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature