Inhibitory profiles of captopril on matrix metalloproteinase-9 activity.
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.
Yamamoto
Daisuke
D
Biomedical Computation Center, Osaka Medical College, 2-7 Daigakuchou, Takatsuki, Osaka 569-8686, Japan. center@art.osaka-med.ac.jp <center@art.osaka-med.ac.jp>
Takai
Shinji
S
Miyazaki
Mizuo
M
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000494:pharmacology*; D001665:Binding Sites; D002216:Captopril / Q000737:chemistry / Q000494:pharmacology*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D020780:Matrix Metalloproteinase 9 / Q000737:chemistry; D061965:Matrix Metalloproteinase Inhibitors; D008958:Models, Molecular
D000806:Angiotensin-Converting Enzyme Inhibitors; D061965:Matrix Metalloproteinase Inhibitors; D002216:Captopril; D020780:Matrix Metalloproteinase 9