New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamases

被引：23

作者：

Yang, Ke-Wu ^{[1
]}

Feng, Lei ^{[1
]}

Yang, Shao-Kang ^{[1
]}

Aitha, Mahesh ^{[2
]}

LaCuran, Alecander E. ^{[3
]}

Oelschlaeger, Peter ^{[3
]}

Crowder, Michael W. ^{[2
]}

机构：

[1] NW Univ Xian, Coll Chem & Mat Sci, Minist Educ, Key Lab Synthet & Nat Funct Mol Chem, Xian 710069, Peoples R China

[2] Miami Univ, Dept Chem & Biochem, Oxford, OH 45056 USA

[3] Western Univ Hlth Sci, Coll Pharm, Dept Pharmaceut Sci, Pomona, CA 91766 USA

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2013年 / 23卷 / 21期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

Metallo-beta-lactamase; Inhibitor; Phospholactam; VANCOMYCIN RESISTANCE; CARBOXYPEPTIDASE-A; MECHANISM; POTENT; HYDROLYSIS; REACTIVITY; IMP-1; ACID; L1; D-; D-DIPEPTIDASE;

D O I：

10.1016/j.bmcl.2013.08.098

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

In an effort to test whether a transition state analog is an inhibitor of the metallo-beta-lactamases, a phospholactam analog of carbapenem has been synthesized and characterized. The phospholactam 1 proved to be a weak, time-dependent inhibitor of IMP-1 (70%), CcrA (70%), L1 (70%), NDM-1 (53%), and Bla2 (94%) at an inhibitor concentration of 100 mu M. The phospholactam 1 activated ImiS and BcII at the same concentration. Docking studies were used to explain binding and to offer suggestions for modifications to the phospholactam scaffold to improve binding affinities. (C) 2013 Elsevier Ltd. All rights reserved.

引用

页码：5855 / 5859

页数：5

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