Differences in structure of angiotensin-converting enzyme inhibitors might predict differences in action.
Angiotensin-converting enzyme (ACE) inhibitors probably work by inhibition of tissue-located ACE, and they differ with regard to their relative ability to inhibit ACE in different organs. This apparent tissue selectivity may stem from either differences in tissue bioavailability or from a different affinity for the enzyme. The affinity of the ACE inhibitor for a particular enzyme is not only determined by the structure of the inhibitor, but also by the structure of the enzyme. ACE enzymes from different tissues may be slightly different, and this may have some bearing on the relative affinities of different ACE inhibitors for ACE from different tissues. The duration of inhibition in a particular tissue reflects not only the affinity of that inhibitor for the tissue enzyme, but also reflects the ease or difficulty with which the active ACE inhibitor is released from that tissue. Whether the beneficial effects of ACE inhibitors on experimentally induced myocardial infarction and reperfusion arrhythmias are due to the presence of a sulfhydryl group or are mainly related to the ACE inhibitor-mediated bradykinin potentiation remains a matter of controversy.
Herman
A G
AG
Division of Pharmacology, University of Antwerp (UIA), Wilrijk, Belgium.
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry* / Q000378:metabolism / Q000493:pharmacokinetics / Q000494:pharmacology*; D000818:Animals; D002216:Captopril / Q000737:chemistry / Q000494:pharmacology; D004151:Dipeptides / Q000737:chemistry / Q000494:pharmacology; D006801:Humans; D017706:Lisinopril
D000806:Angiotensin-Converting Enzyme Inhibitors; D004151:Dipeptides; D002216:Captopril; D017706:Lisinopril