Structures of synthetic helical filaments and tubes based on peptide and peptido-mimetic polymers. (21st March 2022)

• Record Type: Journal Article
• Authors: Miller, Jessalyn G.; Hughes, Spencer A.; Modlin, Charles; Conticello, Vincent P.
• Is Part Of: Quarterly reviews of biophysics. Volume 55(2022)
• Publication Date: 2022-03-21
• Subjects: Cryo-EM -- de novo peptide design -- filament -- helical symmetry -- nanotube -- near-atomic resolution -- peptide self-assembly; Biophysics -- Periodicals; 571.405
• DOI: 10.1017/S0033583522000014
• Languages: English
• ISSNs: 0033-5835

Abstract

Abstract: Synthetic peptide and peptido-mimetic filaments and tubes represent a diverse class of nanomaterials with a broad range of potential applications, such as drug delivery, vaccine development, synthetic catalyst design, encapsulation, and energy transduction. The structures of these filaments comprise supramolecular polymers based on helical arrangements of subunits that can be derived from self-assembly of monomers based on diverse structural motifs. In recent years, structural analyses of these materials at near-atomic resolution (NAR) have yielded critical insights into the relationship between sequence, local conformation, and higher-order structure and morphology. This structural information offers the opportunity for development of new tools to facilitate the predictable and reproducible de novo design of synthetic helical filaments. However, these studies have also revealed several significant impediments to the latter process – most notably, the common occurrence of structural polymorphism due to the lability of helical symmetry in structural space. This article summarizes the current state of knowledge on the structures of designed peptide and peptido-mimetic filamentous assemblies, with a focus on structures that have been solved to NAR for which reliable atomic models are available.