Synthesis and in vitro evaluation of new azaphenylalanine derivatives as serine protease inhibitors

New inhibitors of serine proteases with azaphenylalanine scaffold were synthesized and their activity was evaluated in vitro. We studied the effect of different substituents in the part of a molecule that binds in the distal pocket of the thrombin active site. Modifications generally led to decrease...

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Bibliographic Details
Published in:	Pharmazie Vol. 59; no. 10; p. 739
Main Authors:	Obreza, A, Stegnar, M, Trampus-Bakija, A, Prezelj, A, Urleb, U
Format:	Journal Article
Language:	English
Published:	Germany 01-10-2004
Subjects:	Chromatography, Thin Layer Indicators and Reagents Magnetic Resonance Spectroscopy Mass Spectrometry Phenylalanine - analogs & derivatives Phenylalanine - chemical synthesis Phenylalanine - pharmacology Serine Proteinase Inhibitors - chemical synthesis Serine Proteinase Inhibitors - pharmacology Spectrophotometry, Infrared Structure-Activity Relationship Thiadiazoles - chemical synthesis Thiadiazoles - pharmacology Thrombin - antagonists & inhibitors
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Summary:	New inhibitors of serine proteases with azaphenylalanine scaffold were synthesized and their activity was evaluated in vitro. We studied the effect of different substituents in the part of a molecule that binds in the distal pocket of the thrombin active site. Modifications generally led to decreased activity, however two derivatives are promising lead compounds as new thrombin and dual thrombin-factor Xa inhibitors.
ISSN:	0031-7144