期刊
EUROPEAN JOURNAL OF PHARMACOLOGY
卷 588, 期 2-3, 页码 277-279出版社
ELSEVIER
DOI: 10.1016/j.ejphar.2008.04.031
关键词
matrix metalloproteinase-9; ACE (angiotensin-converting enzyme) inhibitor; molecular structure; inhibitory specificity; myocardial infarction; enzyme activation
To investigate the inhibitory profiles of angiotensin-converting enzyme (ACE) inhibitors on matrix metalloproteinase-9 (MMP-9) activity, the inhibitory activity and molecular interaction of captopril on human MMP-9 were studied. Plasma MMP-9 and ACE activities in samples from patient with acute myocardial infarction were similarly inhibited by captopril. Molecular models showed that captopril directly bound to the MMP-9 active center. Compared with the other ACE inhibitors, the compact structure of captopril seemed to make the inhibitory profiles on the MMP-9 active site. (C) 2008 Elsevier B.V. All rights reserved.
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