## Abstract Peptide‐containing block copolymers poly(__N__‐acetyliminoethylene)‐__block__‐poly(L‐phenylalanine)s (1) form water‐soluble large aggregates in water due to the hydrophobic and hydrogen‐bonding nature of the poly(L‐phenylalanine) block. The solution properties were studied by size exclu
Aggregate of a peptide-containing block copolymer with a lipase
✍ Scribed by Kensuke Naka; Rie Yamashita; Tohru Nakamura; Akira Ohki; Shigeru Maeda; Keigo Aoi; Kaname Tsutsumiuchi; Masahiko Okada
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 311 KB
- Volume
- 17
- Category
- Article
- ISSN
- 1022-1336
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✦ Synopsis
Abstract
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.
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