Investigation of factor Xa inhibitors containing non-amidine S1 elements

Jeffry B Franciskovich; John J Masters; Jennifer M Tinsley; Trelia J Craft; Larry L Froelich; Donetta S Gifford-Moore; Valentine J Klimkowski; Jeffrey K Smallwood; Gerald F Smith; Tommy Smith; Richard R Towner; Leonard C Weir; Michael R Wiley

doi:10.1016/j.bmcl.2005.07.030

Investigation of factor Xa inhibitors containing non-amidine S1 elements

Bioorg Med Chem Lett. 2005 Nov 1;15(21):4838-41. doi: 10.1016/j.bmcl.2005.07.030.

Authors

Jeffry B Franciskovich¹, John J Masters, Jennifer M Tinsley, Trelia J Craft, Larry L Froelich, Donetta S Gifford-Moore, Valentine J Klimkowski, Jeffrey K Smallwood, Gerald F Smith, Tommy Smith, Richard R Towner, Leonard C Weir, Michael R Wiley

Affiliation

¹ Lilly Research Laboratories, Eli Lilly and Company, Lilly Corporate Center, Indianapolis, IN 46285, USA. j.franciskovich@lilly.com

PMID: 16140530
DOI: 10.1016/j.bmcl.2005.07.030

Abstract

Several non-amidino S1 derivatives of the 1,2-diaminobenzene-based scaffold (4) were synthesized and evaluated for their ability to bind to the active site and inhibit the human protease factor Xa. A subset of these compounds were also evaluated for their anticoagulant effects in human plasma as measured by prothrombin time (PT).

MeSH terms

Anticoagulants / chemical synthesis*
Anticoagulants / pharmacology
Benzene Derivatives / chemical synthesis*
Benzene Derivatives / pharmacology
Binding Sites
Blood Coagulation / drug effects
Factor Xa / metabolism
Factor Xa Inhibitors*
Humans
Models, Molecular
Protease Inhibitors / chemical synthesis
Protease Inhibitors / pharmacology
Protein Binding
Prothrombin Time
Structure-Activity Relationship

Substances

Anticoagulants
Benzene Derivatives
Factor Xa Inhibitors
Protease Inhibitors
Factor Xa