Evaluation of the inhibition of other metalloproteinases by matrix metalloproteinase inhibitors

被引：7

作者：

Marcotte, PA ^{[1
]}

Elmore, IN ^{[1
]}

Guan, ZW ^{[1
]}

Magoc, TJ ^{[1
]}

Albert, DH ^{[1
]}

Morgan, DW ^{[1
]}

Curtin, ML ^{[1
]}

Garland, RB ^{[1
]}

Guo, Y ^{[1
]}

Heyman, HR ^{[1
]}

Holms, JH ^{[1
]}

Sheppard, GS ^{[1
]}

Steinman, DH ^{[1
]}

Wada, CK ^{[1
]}

Davidsen, SK ^{[1
]}

机构：

[1] Abbott Labs, Div Pharmaceut Discovery, Canc Res, Abbott Pk, IL 60064 USA

来源：

JOURNAL OF ENZYME INHIBITION | 1999年 / 14卷 / 06期

关键词：

matrix metalloproteinases; MMPs; hydroxamic acid inhibitors;

D O I：

10.3109/14756369909030333

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Two series of compounds synthesized as specific matrix metalloproteinase (MMP) inhibitors have been evaluated for their inhibition of non-MMPs. In a series of substituted succinyl hydroxamic acids, some were found to be significant (IC50 < 1 mu M) inhibitors of leucine (microsomal) aminopeptidase. neprilysin (3.4.24.11), and thermolysin. Macrocyclic compounds in which the alpha carbon of the succinyl hydroxamate is linked to the side chain of the P2' amino acid were found to be good inhibitors of aminopeptidase, but not of neprilysin or thermolysin. Compounds of neither series were found to be significant inhibitors of angiotensin converting enzyme or carboxypeptidase A.

引用

页码：425 / 435

页数：11

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