[Synthetic inhibitors of serine proteinases. 34. The effect of modification of the amidino function of N-alpha-substituted 4-amidinophenylalanine amides on inhibitory activity].
Cyclic amides of N alpha-arylsulfonylated 4-amidinophenylalanine are selective inhibitors of thrombin. The exchange of the amidino function for an aminomethyl residue does not influence the selectivity and potency of their inhibitory activity. In contrast, the modification of the amidino function of the N alpha-arylsulfonylaminoacylated compound N alpha-(2-naphthylsulfonylglycyl)-4-amidinophenylalanine piperidide results in a drastic loss of inhibitory activity. Only the oxamidino derivative possesses considerable high affinity for thrombin. Obviously, in tight binding inhibitors of thrombin structural variation results in any case in a loss of inhibitory activity.
Stürzebecher
J
J
Institut für Pharmakologie und Toxikologie, Medizinischen Akademie Erfurt.
Horn
H
H
Walsmann
P
P
Voigt
B
B
Markwardt
F
F
Wagner
G
G
D000578:Amidines / Q000138:chemical synthesis* / Q000494:pharmacology; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000494:pharmacology; D015842:Serine Proteinase Inhibitors
D000578:Amidines; D015842:Serine Proteinase Inhibitors; D010649:Phenylalanine; D002918:Chymotrypsin
Synthetische Inhibitoren der Serinproteinasen. 34. Mitteilung: Einfluss der Abwandlung der Amidinofunktion bei N alpha-substituierten 4-Amidino-phenylalaninamiden auf die Inhibitoraktivität.