Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 2: Substitution of the glycine part

被引：16

作者：

Amssoms, K

Oza, SL

Augustyns, K

Yamani, A

Lambeir, AM

Bal, G

Van der Veken, P

Fairlamb, AH

Haemers, A ^{[1
]}

机构：

[1] Univ Instelling Antwerp, Dept Med Chem, B-2610 Antwerp, Belgium

[2] Univ Dundee, Dept Biochem, Dundee DD1 4HN, Scotland

[3] Univ Instelling Antwerp, Dept Med Biochem, B-2610 Antwerp, Belgium

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2002年 / 12卷 / 19期

基金：

英国惠康基金;

关键词：

D O I：

10.1016/S0960-894X(02)00538-3

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

Glutathionylspermidine synthetase (GspS) is an essential enzyme in the biosynthesis of trypanothione and is an attractive target for the design of selective anti-parasitic drugs. We synthesised a series of analogues of glutathione (L-gamma-Glu-L-Leu-X) where the glycine moiety has been substituted for other amino acids. These peptides were evaluated as substrates and inhibitors of GspS. Compounds with basic side chains such as diaminopropionic acid were found to be good inhibitors (K-i: 7.2 muM). Substitution of the glycine part abolished the GspS substrate properties of the tripeptide. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：2703 / 2705

页数：3

共 10 条

[1] Glutathione-like tripeptides as inhibitors of glutathionyispermidine synthetase. Part 1: Substitution of the glycine carboxylic acid group [J].