| Autor: |
J L, Krstenansky, R J, Broersma, T J, Owen, M H, Payne, M T, Yates, S J, Mao |
| Rok vydání: |
1990 |
| Předmět: |
|
| Zdroj: |
Thrombosis and haemostasis. 63(2) |
| ISSN: |
0340-6245 |
| Popis: |
MDL 28,050 is a decapeptide antithrombin agent that inhibits alpha-thrombin-induced fibrin clot formation by binding to a non-catalytic site on alpha-thrombin. It is the result of chemical and structural optimization of a functional domain of the leech anticoagulant, hirudin. In contrast to the contention that the polyanionic nature of this C-terminal functional domain governs its interaction with alpha-thrombin, systematic study of this region has shown the importance of the lipophilic residues for providing the functionality necessary for potent binding to alpha-thrombin. The development of MDL 28,050 and other effective antithrombin agents are outlined through the description of the structure-activity relationships (SAR) for these peptides. These peptides are effective in a variety of in vitro and in vivo models of thrombosis. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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