Designing peptide mimetics.
During this century, the nonpeptidic families of hormones (for example, steroids and catecholamines) have been exploited by medicinal chemists to give an array of clinically important drugs. Although peptides represent the largest class of hormonal substances, they are limited in their potential for treating a variety of diseases because of their lack of oral bioavailability and their short durations of action resulting from enzymic degradation in vivo. Recently, rapid screening of small molecule libraries and rational design approaches have produced peptide mimetics as a new generation of promising drug leads. In this review, Graham Moore provides some insight into aspects of the rational design approach to peptide mimicry using angiotensin II as an example.
Department of Pharmacology and Therapeutics, University of Calgary, Alberta, Canada.
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GJ
Moore
D000804:Angiotensin II / Q000031:analogs & derivatives* / Q000037:antagonists & inhibitors; D000959:Antihypertensive Agents / Q000138:chemical synthesis / Q000494:pharmacology; D001665:Binding Sites; D015195:Drug Design; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D010455:Peptides / Q000138:chemical synthesis* / Q000494:pharmacology; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D000959:Antihypertensive Agents; D010455:Peptides; D000804:Angiotensin II