title: Elucidation of a common structure of selective fibrinogen receptor antagonists.
abstract: In this paper, we investigate the common structural and electrostatic parameters of a series of specific inhibitors of the alpha IIb beta 3 integrin. Molecular dynamics simulations with an explicit aqueous environment led to an original theoretical pattern. Our results may suggest that the studied non-peptide alpha IIb beta 3 antagonists developed upon the Arg-Gly-Asp ubiquitous recognition sequence, in fact, should mimic the C-terminus part of the fibrinogen gamma chain. This assumption could, therefore, explain their specificity with respect to other Arg-Gly-Asp-dependent integrins.
authors.affiliation: Groupe Biochimie Théorique, Université Henri Poincaré, Nancy I, Vandoeuvre-lès-Nancy, France.
authors.forename: H
authors.initials: H
authors.lastname: Minoux
authors.forename: N
authors.initials: N
authors.lastname: Moitessier
authors.forename: Y
authors.initials: Y
authors.lastname: Chapleur
authors.forename: B
authors.initials: B
authors.lastname: Maigret
mesh_terms: D000595:Amino Acid Sequence; D008958:Models, Molecular; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry*; D019039:Platelet Glycoprotein GPIIb-IIIa Complex / Q000037:antagonists & inhibitors*; D055672:Static Electricity
chemical_list: D009842:Oligopeptides; D010975:Platelet Aggregation Inhibitors; D019039:Platelet Glycoprotein GPIIb-IIIa Complex; C047981:arginyl-glycyl-aspartic acid