Polymers containing enzymatically degradable bonds, 1. Chymotrypsin catalyzed hydrolysis of p‐nitroanilides of phenylalanine and tyrosine attached to side‐chains of copolymers of N‐(2‐hydroxypropyl)methacrylamide
Polymers containing enzymatically degradable bonds, 1. Chymotrypsin catalyzed hydrolysis of p‐nitroanilides of phenylalanine and tyrosine attached to side‐chains of copolymers of N‐(2‐hydroxypropyl)methacrylamide
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含有可酶降解键的聚合物，1.胰凝乳蛋白酶催化水解连接在N-(2-羟丙基)甲基丙烯酰胺共聚物侧链上的苯丙氨酸和酪氨酸的对硝基苯胺
DOI：
10.1002/macp.1981.021820310
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发表时间：
1981
影响因子：
2.5
通讯作者：
V. Chytrý
中科院分区：
文献类型：
--
作者：
J. Kopeček;P. Rejmanová;V. Chytrý
制备了一系列N-（2-羟丙基）甲基丙烯酰胺的共聚物，其含有通式-Gly-X-Y-NAp的侧链，其中Gly ¨ glyine; X ¨ glyine、alanine、β-alanine、valine、leucine、isoleine、phylalanine; Y ¨ phylalanine或tyrosine; NAp ¨ p-nitroanilide，后者模拟生物活性化合物。在pH = 8.0和25°C下，在一定范围的底物浓度下测定胰凝乳蛋白酶催化的对硝基苯胺基团水解的速率，以得出kcat和KM的值。结果使我们能够确定侧链结构对Y-NAp裂解速率的影响。通过比较含有-Gly-Gly-Phe-Phe-NAp、-Gly-Gly-Phe-NAp和-Gly-Phe-NAp侧链的共聚物的动力学数据，证明了随着Y-NAp残基与聚合物链的主链的间距增加，对糜蛋白酶攻击的敏感性增加。用α-胰凝乳蛋白酶获得的结果与用与N-（2-羟丙基）甲基丙烯酰胺的共聚物共价结合的胰凝乳蛋白酶切割上述聚合物底物的结果进行了比较。
A series of copolymers of N-(2-hydroxypropyl)methacrylamide were prepared, which contained side chains of the general formula -Gly-X-Y-NAp, where Gly ¨ glycine; X ¨ glycine, alanine, β-alanine, valine, leucine, isoleucine, phenylalanine; Y ¨ phenylalanine or tyrosine; NAp ¨ p-nitroanilide, the latter modelling biologically active compounds. The rates of chymotrypsin-catalyzed hydrolysis of p-nitroanilide groups at pH = 8,0 and 25°C were determined over a range of substrate concentrations to derive values for kcat and KM. The results allowed us to determine the influence of the structure of side chains on the rate of cleavage of Y-NAp. The increase in the susceptibility to chymotrypsin attack with an increasing spacing of the Y-NAp residue from the backbone of the polymer chains is demonstrated by comparing the kinetic data of copolymers containing -Gly-Gly-Phe-Phe-NAp, -Gly-Gly-Phe-NAp and -Gly-Phe-NAp side chains. Results obtained with α-chymotrypsin were compared with the cleavage of the above polymer substrates with chymotrypsin covalently bound to a copolymer of N-(2-hydroxypropyl)methacrylamide.