Design of peptide derived amino alcohols as transition-state analog inhibitors of angiotensin converting enzyme

A new amino alcohol modification designed to mimic the putative transition-state of amide bond cleavage by proteolytic enzymes has been incorporated into the scissile bond position of N-benzoyl-Phe-Ala-Pro, a known substrate of angiotensin converting enzyme (ACE). The resulting modified tripeptides...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 126; no. 1; pp. 419 - 426
Main Authors Gordon, E.M., Godfrey, J.D., Pluscec, Jelka, Von Langen, D., Natarajan, S.
Format Journal Article
LanguageEnglish
Published San Diego, CA Elsevier Inc 01.01.1985
Elsevier
Subjects
Amino Alcohols - pharmacology
angiotensin
Angiotensin-Converting Enzyme Inhibitors
Applied sciences
chemical modification
Chemical Phenomena
Chemistry
Exact sciences and technology
N-benzoyl-phenylalanine-alanine-proline
Oligopeptides - pharmacology
Other techniques and industries
Structure-Activity Relationship
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Summary:A new amino alcohol modification designed to mimic the putative transition-state of amide bond cleavage by proteolytic enzymes has been incorporated into the scissile bond position of N-benzoyl-Phe-Ala-Pro, a known substrate of angiotensin converting enzyme (ACE). The resulting modified tripeptides (i.e. 4 ) are shown to be a new class of potent inhibitors of converting enzyme.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(85)90622-9