期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 121, 期 44, 页码 10269-10275出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.7b10085
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资金
- National Science Foundation [DMR-1608725]
- MALDI-TOF MS instrumentation [CHE-1625002]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1625002] Funding Source: National Science Foundation
- Division Of Materials Research
- Direct For Mathematical & Physical Scien [1608725] Funding Source: National Science Foundation
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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