Sequence/structure relationships in aromatic dipeptide hydrogels formed under thermodynamic control by enzyme-assisted self-assembly
Sequence/structure relationships in aromatic dipeptide hydrogels formed under thermodynamic control by enzyme-assisted self-assembly
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DOI：
10.1039/c2sm25224d
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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;Frederix, Pim W. J. M.;Ulijn, Rein V.
肽衍生物的自组装超分子结构通常反映动力学捕获状态，而不是药物学上最有利的结构，这在试图阐明这些系统的分子设计规则时提出了挑战。在这篇文章中，我们使用由氨基酸衍生物的酶促缩合驱动的化学控制的自组装，来阐明形成水凝胶的四种密切相关的Fmoc-二肽-甲酯的化学组成/纳米结构关系; SF，SL，TF和TL。我们证明了四个系统中的每一个都自组装以形成β-片层的扩展阵列，其通过Fmoc部分的π堆叠互锁，但在分子组织中具有细微的差异，如流变学、荧光发射光谱、红外光谱、X射线衍射分析和分子力学最小化所支持的。
Self-assembled supramolecular structures of peptide derivatives often reflect a kinetically trapped state rather than the thermodynamically most favoured structure, which presents a challenge when trying to elucidate the molecular design rules for these systems. In this article we use thermodynamically controlled self-assembly, driven by enzymatic condensation of amino acid derivatives, to elucidate chemical composition/nanostructure relationships for four closely related Fmoc-dipeptide-methyl esters which form hydrogels; SF, SL, TF and TL. We demonstrate that each of the four systems self-assemble to form extended arrays of beta-sheets which interlock via pi-stacking of Fmoc-moieties, yet with subtle differences in molecular organisation as supported by rheology, fluorescence emission spectroscopy, infrared spectroscopy, X-ray diffraction analysis and molecular mechanics minimisation.