Self-assembly of amphiphilic peptides: Effects of the single-chain-to-gemini structural transition and the side chain groups
Self-assembly of amphiphilic peptides: Effects of the single-chain-to-gemini structural transition and the side chain groups
复制标题
两亲性肽的自组装:单链到双子结构转变和侧链基团的影响
DOI:
10.1016/j.colsurfa.2015.01.044
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发表时间:
2015-03-20
影响因子:
5.2
通讯作者:
Xu, Hai
中科院分区:
文献类型:
--
作者:
Cao, Meiwen;Cao, Changhai;Xu, Hai
By designing cysteine-containing single-chain peptides and then linking two such molecules with disulfide bond under oxidation, a series of amphiphilic gemini peptides were successfully synthesized. The gemini geometry introduced not only additional constraints in molecular conformations but also the differentiated intra- and intermolecular hydrogen bonding. These aspects result in specific transition of the self-assembly behavior. The single-chain peptides tended to form spherical aggregates, while the gemini molecules all self-assembled into fiber-like structures, especially that I3C-CI3 could form short thin fibers with highly ordered lateral alignments that are rarely found. Moreover, the self-assembly of both the single-chain and the gemini peptides showed great dependence on the side chain groups. With increasing the size of the side chain alkyl groups, the molecules gave decreased critical aggregation concentration (CAC) and were more ready to arrange into ordered assemblies. This should be ascribed to the enhanced hydrophobic interaction and the subsequent force balance shifts. (C) 2015 Elsevier B.V. All rights reserved.