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Issue 26, 2016
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Catalytic supramolecular self-assembled peptide nanostructures for ester hydrolysis

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Essential amino acids in catalytic sites of native enzymes are important in nature inspired catalyst designs. Active sites of enzymes contain the coordinated assembly of multiple amino acids, and catalytic action is generated by the dynamic interactions among multiple residues. However, catalysis studies are limited by the complex and dynamic structure of the enzyme; and it is difficult to exclusively attribute a given function to a specific residue. Minimalistic approaches involving artificial catalytic sites are promising for the investigation of the enzyme function in the absence of non-essential protein components, and self-assembling peptide nanostructures are especially advantageous in this context. Here we demonstrate the design and characterization of an enzyme-mimetic catalytic nanosystem presenting essential residues (Ser, His, Asp). The function of each residue and its combinations on the nanostructures in hydrolysis reaction was studied. The catalytic self-assembled nanostructures were used for efficient ester hydrolysis such as a model substrate (pNPA) and a natural substrate (acetylcholine) highlighting the key role of self-assembly in catalytic domain formation to test the efficiency of the de novo designed catalyst as a catalytic triad model.

Graphical abstract: Catalytic supramolecular self-assembled peptide nanostructures for ester hydrolysis

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Publication details

The article was received on 30 Mar 2016, accepted on 08 Jun 2016 and first published on 08 Jun 2016

Article type: Paper
DOI: 10.1039/C6TB00795C
Citation: J. Mater. Chem. B, 2016,4, 4605-4611

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    Catalytic supramolecular self-assembled peptide nanostructures for ester hydrolysis

    G. Gulseren, M. A. Khalily, A. B. Tekinay and M. O. Guler, J. Mater. Chem. B, 2016, 4, 4605
    DOI: 10.1039/C6TB00795C

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