In vitro evaluation of synthetic heparin-like conjugates comprising different thrombin binding domains.
The syntheses of several heparin-like glycoconjugates (i.e., 16a-f) containing identical AT III binding domains (ABD) and spacers but different thrombin binding domains (TBDs) are described. Biological activities of conjugates 16a-f indicate that the thrombin inhibitory activity is mainly determined by the charge density of the TBD moiety.
Basten
J E
JE
N.V. Organon Scientific Development Group, The Netherlands.
Dreef-Tromp
C M
CM
de Wijs
B
B
van Boeckel
C A
CA
D000805:Angiotensin III / Q000378:metabolism; D001665:Binding Sites; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D003871:Dermatan Sulfate / Q000737:chemistry; D015195:Drug Design; D006001:Glycoconjugates / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D006493:Heparin / Q000031:analogs & derivatives* / Q000494:pharmacology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013917:Thrombin / Q000378:metabolism*
D006001:Glycoconjugates; D009844:Oligosaccharides; D000805:Angiotensin III; D003871:Dermatan Sulfate; D006493:Heparin; D013917:Thrombin