Ketomethyldipeptides I. A new class of angiotensin converting enzyme inhibitors
The design rationale for a new series of angiotensin-converting enzyme (ACE) inhibitors which incorporate a ketone substituent into a peptide backbone is described. Molecular regions which were expected to mimic the binding of an N-acyl tripeptide substrate at secondary binding sites S 1 and S 1′ we...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1984-10, Vol.124 (1), p.141-147 |
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| container_start_page | 141 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 124 |
| creator | Natarajan, S. Gordon, E.M. Sabo, E.F. Godfrey, J.D. Weller, H.N. Pluščec, Jelka Rom, M.B. Cushman, D.W. |
| description | The design rationale for a new series of angiotensin-converting enzyme (ACE) inhibitors which incorporate a ketone substituent into a peptide backbone is described. Molecular regions which were expected to mimic the binding of an N-acyl tripeptide substrate at secondary binding sites S
1 and S
1′ were systematically varied in order to study the specificity of inhibitor binding and optimize inhibition against ACE. The most effective ketomethyldipeptides inhibit ACE in the 10
−9 M range. |
| doi_str_mv | 10.1016/0006-291X(84)90928-8 |
| format | Article |
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−9 M range.</description><subject>Angiotensin-Converting Enzyme Inhibitors</subject><subject>Biological and medical sciences</subject><subject>Dipeptides - chemical synthesis</subject><subject>Dipeptides - pharmacology</subject><subject>General pharmacology</subject><subject>ketomethyldipeptides</subject><subject>Medical sciences</subject><subject>peptidyl dipeptidase A</subject><subject>Pharmacology. Drug treatments</subject><subject>Physicochemical properties. 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A new class of angiotensin converting enzyme inhibitors</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1984-10-15</date><risdate>1984</risdate><volume>124</volume><issue>1</issue><spage>141</spage><epage>147</epage><pages>141-147</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>The design rationale for a new series of angiotensin-converting enzyme (ACE) inhibitors which incorporate a ketone substituent into a peptide backbone is described. Molecular regions which were expected to mimic the binding of an N-acyl tripeptide substrate at secondary binding sites S
1 and S
1′ were systematically varied in order to study the specificity of inhibitor binding and optimize inhibition against ACE. The most effective ketomethyldipeptides inhibit ACE in the 10
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| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1984-10, Vol.124 (1), p.141-147 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_81321125 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Angiotensin-Converting Enzyme Inhibitors Biological and medical sciences Dipeptides - chemical synthesis Dipeptides - pharmacology General pharmacology ketomethyldipeptides Medical sciences peptidyl dipeptidase A Pharmacology. Drug treatments Physicochemical properties. Structure-activity relationships Protein Binding Stereoisomerism Structure-Activity Relationship |
| title | Ketomethyldipeptides I. A new class of angiotensin converting enzyme inhibitors |
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