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Aggregate of a peptide‐containing block copolymer with a lipase
Author(s) -
Naka Kensuke,
Yamashita Rie,
Nakamura Tohru,
Ohki Akira,
Maeda Shigeru,
Aoi Keigo,
Tsutsumiuchi Kaname,
Okada Masahiko
Publication year - 1996
Publication title -
macromolecular rapid communications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.348
H-Index - 154
eISSN - 1521-3927
pISSN - 1022-1336
DOI - 10.1002/marc.1996.030170409
Subject(s) - copolymer , lipase , polymer chemistry , hydrolysis , phenylalanine , chemistry , hydrogen bond , propionate , hydrophobic effect , block (permutation group theory) , chemical engineering , materials science , organic chemistry , polymer , molecule , amino acid , enzyme , biochemistry , geometry , mathematics , engineering
The peptide‐containing block copolymer poly( N ‐acetyliminoethylene)‐ block ‐poly( L ‐phenylalanine) (1) formed large water‐soluble aggregates in water due to the hydrophobic and hydrogen‐bonding character of the poly( L ‐phenylalanine) block. The solution properties of 1 were compared with those of the block copolymer poly( N ‐acetyliminoethylene)‐ block ‐poly( N ‐benzoyliminoethylene) (2) with an analogous structure. 1 formed aggregates even though the poly(phenylalanine) segment was short as compared with 2 in which hydrophobic interaction may be the only driving force to form aggregates. The aggregates have strong capability of incorporating Lipase P and largely increase the hydrolysis activity against p ‐nitrophenyl propionate as compared with that of free Lipase P.