Tuning of peptide assembly through force balance adjustment.
Tuning of peptide assembly through force balance adjustment.
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DOI：
10.1016/j.jcis.2013.06.051
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发表时间：
2013-10
影响因子：
9.9
通讯作者：
Meiwen Cao;Changhai Cao;Li-juan Zhang;Daohong Xia;Hai Xu
中科院分区：
文献类型：
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作者：
Meiwen Cao;Changhai Cao;Li-juan Zhang;Daohong Xia;Hai Xu
通过分子结构的受控设计，实现两亲性三肽到不同纳米结构的受控自组装。Ac-Phe-Phe-Lys-CONH 2（FFK）是一种难溶于水的三肽，通过β-折叠氢键和芳香π-π堆积形成长的淀粉样管状结构。苯丙氨酸（F）被酪氨酸（Y）取代，即仅在苯环上添加羟基的细微结构变化，导致分子自组装行为的巨大变化。当一个F被Y取代时，所得到的FYK和YFK分子自组装成具有高侧向缔合倾向的长而细的原纤维。当两个F都被Y取代时，所得的YYK分子形成球形聚集体。将羟基基团引入分子中修饰芳族相互作用并引入氢键。此外，由于用于肽自组装的驱动力（包括氢键、静电排斥和π-π堆积）彼此具有高度的相互依赖性，芳香族相互作用的变化诱导多米诺效应，并导致力平衡向新的状态转移。这导致自组装行为的显著变化。
Controlled self-assembly of amphiphilic tripeptides into distinct nanostructures is achieved via a controlled design of the molecular architecture. The tripeptide Ac-Phe-Phe-Lys-CONH2(FFK), hardly soluble in water, forms long amyloid-like tubular structures with the aid ofβ-sheet hydrogen bonding and aromatic π–π stacking. Substitution of phenylalanine (F) with tyrosine (Y), that is, only a subtle structural variation in adding a hydroxyl group to the phenyl ring, results in great change in molecular self-assembly behavior. When one F is substituted with Y, the resulting molecules of FYK and YFK self-assemble into long thinner fibrils with high propensity for lateral association. When both Fs are substituted with Y, the resulting YYK molecule forms spherical aggregates. Introduction of hydroxyl groups into the molecule modifies aromatic interactions and introduces hydrogen bonding. Moreover, since the driving forces for peptide self-assembly including hydrogen bonding, electrostatic repulsion, and π–π stacking have high interdependence with each other, changes in aromatic interaction induce a Domino effect and cause a shift of force balance to a new state. This leads to significant variations in self-assembly behavior.