Deterministic chaos in the self-assembly of β sheet nanotubes from an amphipathic oligopeptide.

ABSTRACT: The self-assembly of designed peptides into filaments and other higher-order structures has been the focus of intense interest because of the potential for creating new biomaterials and biomedical devices. These peptide assemblies have also been used as models for understanding biological processes, such as the pathological formation of amyloid. We investigate the assembly of an octapeptide sequence, Ac-FKFEFKFE-NH₂, motivated by prior studies that demonstrated that this amphipathic β strand peptide self-assembled into fibrils and biocompatible hydrogels. Using high-resolution cryoelectron microscopy (cryo-EM), we are able to determine the atomic structure for two different coexisting forms of the fibrils, containing four and five β sandwich protofilaments, respectively. Surpris

SUBMITTER: Wang F 

PROVIDER: S-EPMC8494133 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature