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Probing the structure-activity relationship of a novel artificial cellobiose hydrolase

文献类型： 外文期刊

作者： He, Xingxing 1 ; Zhang, Fuyuan 1 ; Zhang, Lin 1 ; Zhang, Qiang 1 ; Fang, Guozhen 1 ; Liu, Jifeng 1 ; Wang, Shuo 1 ; Zhang 1 ;

作者机构： 1.Tianjin Univ Sci & Technol, Key Lab Food Nutr & Safety, Minist Educ China, Tianjin 300457, Peoples R China

2.Shandong Acad Agr Sci, Shandong Prov Key Lab Test Technol Food Qual & Sa, Jinan 250100, Peoples R China

期刊名称：JOURNAL OF MATERIALS CHEMISTRY B （ 影响因子：6.331； 五年影响因子：5.726 ）

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收录情况： SCI

摘要： The remarkable catalytic properties of enzymes contribute to their unique 3D structures and arrangement of amino acid residues, which provide a blueprint for the design of artificial enzymes. Here, a series of peptide catalysts (PCs) that mimic the unique orientation and function of beta-glycosyl hydrolases were designed. Transmission electron microscopy (TEM), fluorescence analysis, circular dichroism spectroscopy, X-ray diffraction and computational modeling were used to investigate and compare the relationship of the fibrinous structure of PCs with its glycoside hydrolysis activity. These results indicated that the catalytic activity of PCs was not only related to their amyloid-like structures, but it can also be influenced by the site, species, molecular arrangement and steric hindrance of the amino acid sequence. What's more, this is the first report on peptide-inspired catalysts that mimic the natural cellobiose hydrolases. All this provided insights into the potential use of peptide nanoenzymes in the generation of efficient artificial enzymes.

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