Interplay among Sequence, Folding Propensity, and Bio-Piezoelectric Response in Short Peptides and Peptoids
Interplay among Sequence, Folding Propensity, and Bio-Piezoelectric Response in Short Peptides and Peptoids
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DOI：
10.1021/acs.jpcb.7b10085
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发表时间：
2017-11-09
影响因子：
3.3
通讯作者：
Hutchison, Geoffrey R.
中科院分区：
文献类型：
--
作者：
Marvin, Christopher W.;Grimm, Haley M.;Hutchison, Geoffrey R.
许多生物材料是压电的（即，在施加的电场下机械变形）;然而，这种现象的分子起源仍然不清楚。在基于蛋白质的支架的情况下，一种可能性涉及局部折叠基序对所施加的场的灵活响应。在这里，我们测试这一假设，通过检查在一系列的螺旋肽为基础的低聚物的piezoresponse。通过侧链序列和主链组成的系统性变化来控制折叠倾向。Piezoresponse量化的极性自组装单分子膜上的压电力显微镜。结果表明，骨架刚度是一个重要的决定因素，在肽的机电响应。
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.