Designed histidine-rich peptide self-assembly for accelerating oxidase-catalyzed reactions
作者机构：State Key Laboratory of Organic-Inorganic CompositesKey Lab of Biomedical Materials of Natural Macromolecules(Beijing University of Chemical TechnologyMinistry of Education)Beijing Laboratory of Biomedical MaterialsBeijing University of Chemical TechnologyBeijing 100029China
出 版 物：《Nano Research》 (纳米研究（英文版）)
年 卷 期：2022年第15卷第5期
页 面：4032-4038页
核心收录：
学科分类：081704[工学-应用化学] 07[理学] 070304[理学-物理化学(含∶化学物理)] 08[工学] 0817[工学-化学工程与技术] 0703[理学-化学]
基 金：The authors are grateful for Fundamental Research Funds for the Central Universities(Nos.XK1806 and buctrc201902) the financial support from the National Natural Science Foundation of China(Nos.21872044 and 52173194)
主 题：self-assembly oligohistidine enzymes biocatalysis active site
摘 要：It is an important goal for supramolecular chemistry to develop synthetic enzyme mimics rivaling native enzymes,while de novo fabrication of such mimics remains a ***,the catalytic groups from the supramolecular complex can be integrated with the active sites of natural ***,we present a supramolecular catalytic hybrid that is self-assembled from oligohistidine-based peptides and a heme-dependent *** results indicate that the peptides altered the enzyme conformation,promoted the transitions between the resting and the intermediate states of the heme,and increased the turnover rate of the enzyme by up to *** propose that the histidine residues from the peptides may collaborate with the groups in the natural heme pocket to accelerate the catalytic cycles of the *** observations underline the advantages of the supramolecular approach and suggest that molecular self-assembly may combine with enzymes to provide a simple strategy to engineer the enzymatic active sites.
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