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Issue 26, 2017
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Probing the structure–activity relationship of a novel artificial cellobiose hydrolase

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Abstract

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 β-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.

Graphical abstract: Probing the structure–activity relationship of a novel artificial cellobiose hydrolase

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Publication details

The article was received on 25 May 2017, accepted on 07 Jun 2017 and first published on 08 Jun 2017


Article type: Paper
DOI: 10.1039/C7TB01426K
Citation: J. Mater. Chem. B, 2017,5, 5225-5233
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    Probing the structure–activity relationship of a novel artificial cellobiose hydrolase

    X. He, F. Zhang, L. Zhang, Q. Zhang, G. Fang, J. Liu, S. Wang and S. Zhang, J. Mater. Chem. B, 2017, 5, 5225
    DOI: 10.1039/C7TB01426K

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