Bioorganic and Medicinal Chemistry Letters p. 2387 - 2392 (1996)
Update date:2022-09-26
Topics:
Wiley, Michael R.
Chirgadze, Nickolay Y.
Clawson, David K.
Craft, Trelia J.
Gifford-Moore, Donetta S.
Jones, Noel D.
Olkowski, Jennifer L.
Weir, Leonard C.
Smith, Gerald F.
The design, synthesis, and enzyme inhibitory profile of D-Phe-Pro-p-Amidinobenzylamine are presented. This compound has inhibitory activity equivalent to D-Phe-Pro-Arg-H, two orders of magnitude more potent than D-Phe-Pro-Agmatine. The results indicate that binding energy provided by the covalent bond of a transition-state analog can be replaced with noncovalent interactions.
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Doi:10.1246/bcsj.54.2065
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(1996)
