Interplay among Sequence, Folding Propensity, and Bio-Piezoelectric Response in Short Peptides and Peptoids

Many biomaterials are piezoelectric (i.e., mechanically deform under an applied electric field); however, the molecular origin of this phenomenon remains unclear. In the case of protein-based scaffolds, one possibility involves flexible response of local folding motifs to the applied field. Here, we...

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Bibliographic Details
Published in:The journal of physical chemistry. B 2017-11, Vol.121 (44), p.10269-10275
Main Authors: Marvin, Christopher W, Grimm, Haley M, Miller, Nathaniel C, Horne, W. Seth, Hutchison, Geoffrey R
Format: Article
Language:English
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Summary:Many biomaterials are piezoelectric (i.e., mechanically deform under an applied electric field); however, the molecular origin of this phenomenon remains unclear. In the case of protein-based scaffolds, one possibility involves flexible response of local folding motifs to the applied field. Here, we test this hypothesis by examining the piezoresponse in a series of helical peptide-based oligomers. Control over folding propensity is exerted through systematic variation in both side-chain sequence and backbone composition. Piezoresponse is quantified by piezo-force microscopy on polar self-assembled monolayers. The results indicate backbone rigidity is an important determinant in peptide electromechanical responsiveness.
ISSN:1520-6106
1520-5207
DOI:10.1021/acs.jpcb.7b10085