title: Nonpeptide glycoprotein IIB/IIIA inhibitors. 19. A new design paradigm employing linearly minimized, centrally constrained, exosite inhibitors.
abstract: A new series of potent, linearly-minimized, orally active, selective GPIIb/IIIa inhibitors is identified. Thus 15 (L-750,034) achieves interaction via a constrained, non-turned conformation that maintains the proper distance between its charged termini and full sulfonamide exosite interaction. The diminutive stature and the proposed linear conformation of L-750,034 define a new paradigm for the conceptualization of RGD mimics.
authors: Department of Medicinal Chemistry, Merck Research Laboratories, West Point, PA 19486, USA.
authors: G D
authors: GD
authors: Hartman
authors: M E
authors: ME
authors: Duggan
authors: W F
authors: WF
authors: Hoffman
authors: R J
authors: RJ
authors: Meissner
authors: J J
authors: JJ
authors: Perkins
authors: A E
authors: AE
authors: Zartman
authors: A M
authors: AM
authors: Naylor-Olsen
authors: J J
authors: JJ
authors: Cook
authors: J D
authors: JD
authors: Glass
authors: R J
authors: RJ
authors: Lynch
authors: G
authors: G
authors: Zhang
authors: R J
authors: RJ
authors: Gould
mesh_terms: D001549:Benzamides / Q000494:pharmacology*; D015195:Drug Design; D020128:Inhibitory Concentration 50; D008956:Models, Chemical; D008958:Models, Molecular; D019039:Platelet Glycoprotein GPIIb-IIIa Complex / Q000037:antagonists & inhibitors*; D013997:Time Factors
chemical_list: D001549:Benzamides; D019039:Platelet Glycoprotein GPIIb-IIIa Complex; C103544:4-hydroxybenzamide