超分子化学
脱磷
化学
两亲性
肽
能源景观
生物物理学
自组装
折叠(DSP实现)
蛋白质折叠
磷酸化
纳米技术
生物化学
结晶学
材料科学
磷酸酶
有机化学
聚合物
晶体结构
共聚物
工程类
电气工程
生物
作者
Junfeng Shi,Galit Fichman,Joel P. Schneider
标识
DOI:10.1002/anie.201803983
摘要
Post-translational modification is a common mechanism to affect conformational change in proteins, which in turn, regulates function. Herein, this principle is expanded to instruct the formation of supramolecular assemblies by controlling the conformational bias of self-assembling peptides. Biophysical and mechanical studies show that an engineered phosphorylation/dephosphorylation couple can affectively modulate the folding of amphiphilic peptides into a conformation necessary for the formation of well-defined fibrillar networks. Negative design principles based on the incompatibility of hosting residue side-chain point charge within hydrophobic environments proved key to inhibiting the peptide's ability to adopt its low energy fold in the assembled state. Dephosphorylation relieves this restriction, lowers the energy barrier between unfolded and folded peptide, and allows the formation of self-assembled fibrils that contain the folded conformer, thus ultimately enabling the formation of a cytocompatible hydrogel material.
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