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• W2766276720 startingPage "10269" @default.
• W2766276720 abstract "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." @default.
• W2766276720 created "2017-11-10" @default.
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• W2766276720 date "2017-10-30" @default.
• W2766276720 modified "2023-10-12" @default.
• W2766276720 title "Interplay among Sequence, Folding Propensity, and Bio-Piezoelectric Response in Short Peptides and Peptoids" @default.
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• W2766276720 doi "https://doi.org/10.1021/acs.jpcb.7b10085" @default.
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• W2766276720 hasPublicationYear "2017" @default.
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