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Catalytic Peptide Synthesis by Trypsin Modified with Polystyrene in Chloroform
Author(s) -
Ito Yoshihiro,
Fujii Hajime,
Imanishi Yukio
Publication year - 1993
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp00020a003
Subject(s) - chemistry , polystyrene , trypsin , catalysis , chloroform , styrene , polymer chemistry , organic chemistry , amino acid , polymerization , peptide , polymer , peptide synthesis , copolymer , enzyme , biochemistry
Trypsin was modified with a hydrophobic synthetic polymer, polystyrene. The attachment was achieved by first coupling free amines in the trypsin with azobis(4‐cyanovaleric acid) and then irradiating the product in the presence of styrene. Decomposition of the azo structure provided free radical initiation of styrene polymerization, with the trypsin thus becoming part of the end group for the polymer chain initiated. That the modified trypsin retained catalytic activity when dissolved in chloroform was demonstrated by using it to catalyze the formation of a peptide linkage between amino acids. The catalytic reaction was stereoselective.