Zhao Yanan, Lei Bingqian, Wang Mengfan, Wu Shengtang, Qi Wei, Su Rongxin, He Zhimin
School of Chemical Engineering and Technology, State Key Laboratory of Chemical Engineering, Tianjin University, Tianjin 300350, P. R. China.
J Mater Chem B. 2018 Apr 28;6(16):2444-2449. doi: 10.1039/c8tb00448j. Epub 2018 Apr 11.
In this study, a peptide-based artificial hydrolase with photo-switchable activity was fabricated by the introduction of a catalytic histidine residue and a photo-responsive azobenzene group into the peptide chain. The peptide exhibits a structural transition from an antiparallel β-sheet to a random coil upon photo-irradiation, leading to the assembly/disassembly of the peptide fibril. An enhanced catalytic activity on p-nitrophenyl acetate was observed due to the proximity effect of the histidine residues and the hydrophobic microenvironment in the supramolecular assemblies. Under UV irradiation, this supramolecular system was destroyed together with a decline in the catalytic activity. Based on these photo-responsive properties, the activity of the hydrolase mimic can be reversibly controlled using UV and visible light. This study provides a new approach for constructing a switchable artificial enzyme based on a peptide material platform.
在本研究中，通过将催化性组氨酸残基和光响应性偶氮苯基团引入肽链，制备了一种具有光开关活性的基于肽的人工水解酶。该肽在光照射下呈现从反平行β-折叠到无规卷曲的结构转变，导致肽纤维的组装/解组装。由于组氨酸残基的邻近效应和超分子组装体中的疏水微环境，观察到对乙酸对硝基苯酯的催化活性增强。在紫外线照射下，该超分子体系被破坏，同时催化活性下降。基于这些光响应特性，水解酶模拟物的活性可以通过紫外线和可见光进行可逆控制。本研究为基于肽材料平台构建可切换人工酶提供了一种新方法。
