Catalytic supramolecular self-assembled peptide nanostructures for ester hydrolysis
Date
2016Source Title
Journal of Materials Chemistry B
Print ISSN
2050-7518
Publisher
Royal Society of Chemistry
Volume
4
Issue
26
Pages
4605 - 4611
Language
English
Type
ArticleItem Usage Stats
287
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400
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Abstract
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.
Keywords
Amino acidsBiomimetics
Catalysts
Enzymes
Esters
Hydrolysis
Peptides
Self assembly
Dynamic interaction
Dynamic structure
Essential amino acids
Hydrolysis reaction
Natural substrates
Self assembled nanostructures
Self-assembled peptides
Self-assembling peptides
Nanostructures
Permalink
http://hdl.handle.net/11693/36666Published Version (Please cite this version)
https://doi.org/10.1039/c6tb00795cCollections
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