Differential supramolecular organisation of Fmoc-dipeptides with hydrophilic terminal amino acid residues by biocatalytic self-assembly
Differential supramolecular organisation of Fmoc-dipeptides with hydrophilic terminal amino acid residues by biocatalytic self-assembly
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DOI：
10.1039/c2sm26092a
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发表时间：
2012-01-01
期刊：
影响因子：
3.4
通讯作者：
Ulijn, Rein V.
中科院分区：
文献类型：
--
作者：
Hughes, Meghan;Birchall, Louise S.;Ulijn, Rein V.
近年来，芳香族肽两亲物的酶促自组装研究越来越受欢迎，并导致了各种纳米结构。由于疏水相互作用已被认为是其自组装的主要驱动力，通常，发现肽组分本质上是疏水的，含有芳族或脂族氨基酸残基。在这篇文章中，我们使用枯草杆菌蛋白酶引发的自组装四个密切相关的Fmoc-二肽两亲分子与末端亲水性氨基酸残基，YT，YS，YN和YQ，为了引入一个新的功能的自组装系统，并确定每个氨基酸侧链的影响。我们使用显微镜技术，流变学，荧光，FTIR和CD来展示分子组装，机械性能和纳米级结构的差异，作为每个系统的微妙分子变化的直接结果。我们证明，在位置2的氨基酸侧链直接影响的超分子结构中的分子包装能力，与YT，YS和YN形成纳米纤维的机械性能被链接到氨基酸侧链的功能，和YQ形成球形结构，由于空间效应与谷氨酰胺侧链禁止通过典型的π-β组装。
The study of enzymatically triggered self-assembly of aromatic peptide amphiphiles has become increasingly popular in recent years and has lead to a variety of nanoscale architectures. As hydrophobic interactions have been recognised as a major driving force in their self-assembly, typically, the peptide components are found to be hydrophobic in nature, containing aromatic or aliphatic amino acid residues. In this article, we use subtilisin triggered self-assembly of four closely related Fmoc-dipeptide amphiphiles with terminal hydrophilic amino acid residues, YT, YS, YN and YQ, in order to introduce a new functionality to the self-assembled systems, and determine the influence of each amino acid side chain. We use microscopy techniques, rheology, fluorescence, FTIR and CD to demonstrate differences in molecular assembly, mechanical properties and nanoscale architecture as a direct result of the subtle molecular variance of each system. We demonstrate that the amino acid side chain in position two directly affects the molecular packing abilities in the supramolecular structure, with YT, YS and YN forming nanoscale fibres with mechanical properties being linked to the functionality of the amino acid side chain, and YQ forming spherical structures due to steric effects associated with the glutamine side chain prohibiting the adoption of the typical pi-beta assembly.