Structural analysis of cross α-helical nanotubes provides insight into the designability of filamentous peptide nanomaterials.

ABSTRACT: The exquisite structure-function correlations observed in filamentous protein assemblies provide a paradigm for the design of synthetic peptide-based nanomaterials. However, the plasticity of quaternary structure in sequence-space and the lability of helical symmetry present significant challenges to the de novo design and structural analysis of such filaments. Here, we describe a rational approach to design self-assembling peptide nanotubes based on controlling lateral interactions between protofilaments having an unusual cross-α supramolecular architecture. Near-atomic resolution cryo-EM structural analysis of seven designed nanotubes provides insight into the designability of interfaces within these synthetic peptide assemblies and identifies a non-native structural interaction based on

SUBMITTER: Wang F 

PROVIDER: S-EPMC7814010 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature