| Autor: |
Lumma, W. C., Jr., Witherup, K. M., Tucker, T. J., Brady, S. F., Sisko, J. T., Naylor-Olsen, A. M., Lewis, S. D., Lucas, B. J., Vacca, J. P. |
| Zdroj: |
Journal of Medicinal Chemistry; March 26, 1998, Vol. 41 Issue: 7 p1011-1013, 3p |
| Abstrakt: |
Study of surface representations of the inhibitor-bound thrombin P-1 pocket revealed a lipophilic recess in this pocket which is not occupied by any known inhibitor. Solid-phase synthesis was used to generate benzylamides of d-diphenylAlaPro by aminolysis of Boc dipeptide Kaiser resin. The resulting amides inhibited thrombin in the range IC50 = 3−13 000 nM, and the structure−activity relationships and molecular modeling suggest a unique fit of the benzyl side chain into P-1 with the meta substituent occupying the recess. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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