Biocatalytic induction of supramolecular order
Biocatalytic induction of supramolecular order
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DOI：
10.1038/nchem.861
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发表时间：
2010-12-01
期刊：
影响因子：
21.8
通讯作者：
Ulijn, Rein V.
中科院分区：
文献类型：
--
作者：
Hirst, Andrew R.;Roy, Sangita;Ulijn, Rein V.
超分子凝胶具有可调节的功能，引起了医疗保健、环境保护和能源相关技术等一系列领域的广泛关注。以可靠的方式制备这些材料具有挑战性，在较高的自组装速率下观察到的动力学缺陷水平增加。在这里，通过结合生物催化和分子自组装，我们展示了更快地获得更高阶结构的能力。通过简单地增加酶浓度，在分子、纳米和微米水平上表达的超分子秩序显着增强，而且重要的是，胶凝剂浓度保持不变。两亲分子是通过将芳香族部分连接到用甲酯封端的二肽主链上来制备的。它们的自组装是由水解酯的酶诱导的。不同的酶浓度改变了酶簇的催化活性和大小，从而影响了它们的迁移率。这使得可以基于单一胶凝剂结构来访问代表自由能景观中局部最小值的结构多样的材料。
Supramolecular gels, which demonstrate tunable functionalities, have attracted much interest in a range of areas, including healthcare, environmental protection and energy-related technologies. Preparing these materials in a reliable manner is challenging, with an increased level of kinetic defects observed at higher self-assembly rates. Here, by combining biocatalysis and molecular self-assembly, we have shown the ability to more quickly access higher-ordered structures. By simply increasing enzyme concentration, supramolecular order expressed at molecular, nano- and micro-levels is dramatically enhanced, and, importantly, the gelator concentrations remain identical. Amphiphile molecules were prepared by attaching an aromatic moiety to a dipeptide backbone capped with a methyl ester. Their self-assembly was induced by an enzyme that hydrolysed the ester. Different enzyme concentrations altered the catalytic activity and size of the enzyme clusters, affecting their mobility. This allowed structurally diverse materials that represent local minima in the free energy landscape to be accessed based on a single gelator structure.