New tripeptidic thrombin inhibitors. Influence of P2 and P3 residues on activity and selectivity.
Structural variations of P2 and P3 residues in tripeptidic boroarginine thrombin inhibitors led to compounds with similar potency than reference compound DuP 714, but with enhanced selectivity for thrombin compared to plasmin.
De Nanteuil
G
G
Division of Medicinal Chemistry, Institut de Recherche Servier, Suresnes, France.
Gloanec
P
P
Lila
C
C
Portevin
B
B
Boudon
A
A
Rupin
A
A
Verbeuren
T J
TJ
D000595:Amino Acid Sequence; D000991:Antithrombins / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D001120:Arginine / Q000031:analogs & derivatives; D001665:Binding Sites; D001896:Boron Compounds / Q000737:chemistry / Q000494:pharmacology; D005341:Fibrinolysin / Q000494:pharmacology; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013917:Thrombin / Q000037:antagonists & inhibitors*
D000991:Antithrombins; D001896:Boron Compounds; D009842:Oligopeptides; C066061:acetylphenylalanyl-prolyl-boroarginine; D001120:Arginine; D013917:Thrombin; D005341:Fibrinolysin