Design of highly potent noncovalent thrombin inhibitors that utilize a novel lipophilic binding pocket in the thrombin active site

J Med Chem. 1997 Mar 14;40(6):830-2. doi: 10.1021/jm960762y.

Authors

T J Tucker¹, W C Lumma, A M Mulichak, Z Chen, A M Naylor-Olsen, S D Lewis, R Lucas, R M Freidinger, L C Kuo

Affiliation

¹ Department of Medicinal Chemistry, Merck Research Laboratories, West Point, Pennsylvania 19486, USA.

PMID: 9083470
DOI: 10.1021/jm960762y

No abstract available

MeSH terms

Binding Sites
Crystallography, X-Ray
Cyclohexylamines / chemical synthesis
Cyclohexylamines / chemistry
Cyclohexylamines / metabolism
Cyclohexylamines / pharmacology
Dipeptides / chemical synthesis
Dipeptides / chemistry*
Dipeptides / metabolism
Dipeptides / pharmacology
Drug Design*
Fibrinolytic Agents / chemical synthesis
Fibrinolytic Agents / chemistry*
Fibrinolytic Agents / metabolism
Fibrinolytic Agents / pharmacology
Hydrogen Bonding
Molecular Structure
Protein Binding
Thrombin / antagonists & inhibitors*
Thrombin / chemistry
Thrombin / metabolism

Substances

Cyclohexylamines
Dipeptides
Fibrinolytic Agents
Thrombin