| Abstract
| - The mechanism of inhibition of peptidyl inhibitors with thrombinwas studied using molecularmodeling, molecular mechanics, and CoMFA statistical analysis. Anew procedure for theelucidation of binding conformations, BCSPL, is described and wasemployed to obtain thebinding conformers of a series of 18 tripeptidyl thrombin inhibitors.Energetic studies andQSAR analysis of the BCSPL-derived conformers indicated a modestcorrelation between thecalculated binding energies of the title compounds and their inhibitoryactivities to humanα-thrombin. CoMFA analysis of the BCSPL alignment resulted in asatisfactory model of thethrombin active site.
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