The predominant roles of the sequence periodicity in the self-assembly of collagen-mimetic mini-fibrils.

ABSTRACT: Collagen fibrils represent a unique case of protein folding and self-association. We have recently successfully developed triple-helical peptides that can further self-assemble into collagen-mimetic mini-fibrils. The 35 nm axially repeating structure of the mini-fibrils, which is designated the d-period, is highly reminiscent of the well-known 67 nm D-period of native collagens when examined using TEM and atomic force spectroscopy. We postulate that it is the pseudo-identical repeating sequence units in the primary structure of the designed peptides that give rise to the d-period of the quaternary structure of the mini-fibrils. In this work, we characterize the self-assembly of two additional designed peptides: peptide Col877 and peptide Col108rr. The triple-helix domain of Col877 consists

SUBMITTER: Chen F 

PROVIDER: S-EPMC6699095 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature