Investigation of the terminal P4 domain in a series of d-phenylglycinamide-based factor Xa inhibitors

Autor:	Gerald F. Smith, Wayne W. Weber, John Walter Nr Macclesfield Liebeschuetz, Philip Sipes, Jeffry Bernard Franciskovich, Richard D. Towner, John Joseph Masters, Donetta S. Gifford-Moore, Trelia J. Craft, Ronald S. Foster, Jeffrey K. Smallwood, Michael L. Chouinard, Lea M. Johnson, Larry L. Froelich, Stephen C. Young, David W. Snyder, Marcia K. Chastain, Valentine J. Klimkowski, Christopher W. Murray
Rok vydání:	2007
Předmět:	Models Molecular medicine.drug_mechanism_of_action Stereochemistry Antithrombin III Clinical Biochemistry Factor Xa Inhibitor Glycine Pharmaceutical Science Crystallography X-Ray Biochemistry Chemical synthesis Structure-Activity Relationship In vivo Drug Discovery medicine Humans Molecular Biology Indole test Serine protease chemistry.chemical_classification Molecular Structure biology Chemistry Organic Chemistry Anticoagulants In vitro Enzyme Enzyme inhibitor Factor Xa biology.protein Molecular Medicine Protein Binding
Zdroj:	Bioorganic & Medicinal Chemistry Letters. 17:6910-6913
ISSN:	0960-894X
DOI:	10.1016/j.bmcl.2007.09.105
Popis:	Several P4 domain derivatives of the general d-phenylglycinamide-based scaffold (2) were synthesized and evaluated for their ability to bind to the serine protease factor Xa. Some of the more potent compounds were evaluated for their anticoagulant effects in vitro. A select subset containing various P1 indole constructs was further evaluated for their pharmacokinetic properties after oral administration to rats.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f7308733752c4e2e7235ca66a8d4df0 https://doi.org/10.1016/j.bmcl.2007.09.105 Zobrazit plný text záznamu Full Text from ScienceDirect