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

Fengbin Wang, Ordy Gnewou, Charles Modlin, Leticia C. Beltran, Chunfu Xu, Zhangli Su, Puneet Juneja, Gevorg Grigoryan, Edward H. Egelman and Vincent P. Conticello ()
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Fengbin Wang: University of Virginia
Ordy Gnewou: Emory University
Charles Modlin: Emory University
Leticia C. Beltran: University of Virginia
Chunfu Xu: Emory University
Zhangli Su: University of Virginia
Puneet Juneja: Emory University
Gevorg Grigoryan: Dartmouth College
Edward H. Egelman: University of Virginia
Vincent P. Conticello: Emory University

Nature Communications, 2021, vol. 12, issue 1, 1-14

Abstract: 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 a pair of arginine residues. This arginine clasp motif can robustly mediate cohesive interactions between protofilaments within the cross-α nanotubes. The structure of the resultant assemblies can be controlled through the sequence and length of the peptide subunits, which generates synthetic peptide filaments of similar dimensions to flagella and pili.

Date: 2021
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DOI: 10.1038/s41467-020-20689-w

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