卡托普利
化学
半胱氨酸
IC50型
抗生素
细菌
新德里
效力
酶
生物化学
药理学
微生物学
体外
生物
医学
大都市区
病理
内分泌学
血压
遗传学
作者
Cui‐Gai Bai,Yintong Xu,Ningning Li,Jinghan Wang,Cheng Yang,Yue Chen,Honggang Zhou
出处
期刊:Current Enzyme Inhibition
[Bentham Science Publishers]
日期:2015-04-15
卷期号:11 (1): 46-57
被引量:6
标识
DOI:10.2174/1573408011666150408223245
摘要
Nearly all antibiotics are ineffective to the antibiotic-resistant bacteria New Delhi metallo-beta -lactamase-1(NDM-1), one of the most important reasons is that antibiotics can be hydrolyzed by NDM-1 in these bacteria. Up to date, Many compounds, including captopril, are found to possess NDM-1 inhibition activity. Herein we report that some cysteine derivatives or homocysteine derivatives can inhibit the NDM-1 protein, and the lead compound 9 has the inhibition of the NDM-1 protein with IC50 of 1 µM, which is about 8 times potency of captopril. Keywords: IC50, NDM-1, cysteine, captopril, derivatives, inhibition.
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