| Autor: |
Dillard, R. D., Bach, N. J., Draheim, S. E., Berry, D. R., Carlson, D. G., Chirgadze, N. Y., Clawson, D. K., Hartley, L. W., Johnson, L. M., Jones, N. D., McKinney, E. R., Mihelich, E. D., Olkowski, J. L., Schevitz, R. W., Smith, A. C., Snyder, D. W., Sommers, C. D., Wery, J.-P. |
| Zdroj: |
Journal of Medicinal Chemistry; December 20, 1996, Vol. 39 Issue: 26 p5137-5158, 22p |
| Abstrakt: |
As reported in our previous paper, a series of indole-3-acetamides which possessed potency and selectivity as inhibitors of human nonpancreatic secretory phospholipase A2(hnps-PLA2) was developed. The design of these compounds was based on information derived from x-ray crystal structures determined for complexes between the enzyme and its inhibitors. We describe here the further implementation of this structure-based design strategy and continued SAR development to produce indole-3-acetamides with additional functionalities which provide increased interaction with important residues within the enzyme active site. These efforts led to inhibitors with substantially enhanced potency and selectivity. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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