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Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Interplay among Sequence, Folding Propensity, and Bio-Piezoelectric Response in Short Peptides and Peptoids.
Journal of Physical Chemistry. B 2017 November 10
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.
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