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Reference type: Journal
Authors: Mathew D, Thomas B, Devaky KS
Article Title: Substrate Specific Amidolysis of p-Nitroanilides of Amino Acids using Phosphonate Analogue Imprinted Chymotrypsin Mimics.
Publication date: 2016
Journal: SB Academic Review
Volume: 19
Issue: (1)
Page numbers: 41-49.
Alternative URL: http://sbjournals.com/index.php/sbreview/article/view/6

Abstract: Focusing on bio-recognition, highly crosslinked TSA–built-polymer catalysts were synthesized as chymotrypsin mimics by molecular imprinting technique for substrate specific amidolysis of pnitroanilide of amino acids based on the principle of cooperative catalysis. The polymers having enzyme-like behaviour were prepared using methacryloyl-L-histidine, methacryloyl-L-aspartic acid and 4-vinylpyridine as the functional monomers, phenyl-1-(N-benzyloxy carbonylamino)-2-(phenyl) ethyl phosphonate, the analogue of transition state of amide hydrolysis as the template and methacrylic crosslinker EGDMA as the crosslinking agent. The easy insertion of the substrate followed by selective stabilization of the T.S of amidolysis in the "3-D memorized cavity" in the polymer matrix is responsible for the enhanced substrate specificity of the imprinted chymotrypsin mimics. Cost effective synthesis, ease of preparation, high thermal stability, reusability and higher shelf life make the enzyme mimics highly efficient.
Template and target information: phenyl-1-(N-benzyloxy carbonylamino)-2-(phenyl) ethyl phosphonate, transition state analogue
Author keywords: chymotrypsin mimics, bio-recognition, transition state analogue, 3-D memorized cavity, Amidase activity


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