Structure-activity relationships of substituted benzothiophene-anthranilamide factor Xa inhibitors

Autor:	Brian D. Griedel, Keith Eagen, Shung C. Wu, Morrissey Michael M, Yuo-Ling Chou, Karna Lyn Sacchi, Lan Trinh, David D. Davey, Kenneth J. Shaw, Karanjawala Rushad E, Dao Lentz, Kochanny Monica, Amy Liang, Gary Phillips
Rok vydání:	2003
Předmět:	Serine Proteinase Inhibitors medicine.drug_mechanism_of_action Stereochemistry medicine.drug_class Clinical Biochemistry Factor Xa Inhibitor Pharmaceutical Science Carboxamide Thiophenes Biochemistry chemistry.chemical_compound Structure-Activity Relationship Thrombin Aniline Heterocyclic Compounds Drug Discovery Anthranilic acid medicine Structure–activity relationship Animals Humans ortho-Aminobenzoates Molecular Biology Bicyclic molecule Organic Chemistry Benzothiophene Anticoagulants Kinetics chemistry Prothrombin Time Molecular Medicine Cattle Indicators and Reagents Trypsin Inhibitors medicine.drug Factor Xa Inhibitors
Zdroj:	Bioorganicmedicinal chemistry letters. 13(3)
ISSN:	0960-894X
Popis:	Compound 1 was identified by high throughput screening as a novel, potent, non-amidine factor Xa inhibitor with good selectivity against thrombin and trypsin. A series of modifications of the three aromatic groups of 1 was investigated. Substitution of chlorine or bromine for fluorine on the aniline ring led to the discovery of subnanomolar factor Xa inhibitors. Positions on the anthranilic acid ring that can accommodate further substitution were also identified.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0eac456c84cdeb71df61707321081b28 https://pubmed.ncbi.nlm.nih.gov/12565961 Zobrazit plný text záznamu Full Text from ScienceDirect