Design, synthesis and SAR of RGD peptide hybrids as highly efficient inhibitors of platelet aggregation

  title={Design, synthesis and SAR of RGD peptide hybrids as highly efficient inhibitors of platelet aggregation},
  author={Iwao Ojima and Qing Dong and Subrata Chakravarty and Ellinor I. Peerschke and Shing Mei Hwang and Angela S. Wong},
  journal={Bioorganic \& Medicinal Chemistry Letters},
  • I. Ojima, Q. Dong, A. Wong
  • Published 7 September 1995
  • Biology, Chemistry
  • Bioorganic & Medicinal Chemistry Letters
Design and Synthesis of RGD Mimetics as Potent Inhibitors of Platelet Aggregation
Through a process of rational design, mimetics of the RGD sequence were synthesized, providing deeper insight into the structural requirements for high inhibitory activity, and these mimetics were found to be extremely potent inhibitors of platelet aggregation.
A Constrained Diketopiperazine as a New Scaffold for the Synthesis of Peptidomimetics
The synthesis of new peptidomimetics of the Arg-Gly-Asp (RGD) sequence is described, which shows a selective platelet-aggregation inhibiting activity and can be used as a lead for the preparation of more potent products.
Design, Virtual Screening, and Synthesis of Antagonists of αIIbβ3 as Antiplatelet Agents.
Design, virtual screening, synthesis, and biological tests of novel αIIbβ3 antagonists, which inhibit platelet aggregation are described, which showed that two designed ligands for the open form 4c and 4d were more potent than commercial antithrombotic Tirofiban.
Computer-aided design of novel antithrombotic agents
The computer-aided design of new anti-thrombotic agents able to inhibit two types of receptors located on the surface of the platelets to suggest new potential antagonists of αIIbβ3 and thromboxane A2 receptors.
Molecular dynamics study of disulfide bond influence on properties of an RGD peptide.
  • Y. Wang, S. Goh, K. Kuczera
  • Chemistry, Biology
    The journal of peptide research : official journal of the American Peptide Society
  • 1999
Three 1 ns length molecular dynamics simulations of an RGD peptide (Ac-Pen-Arg-Gly-Asp-Cys-NH2, with Pen denoting penicillamine) have been performed in aqueous solution to calculate several properties and to identify conformations explored by the two forms and to describe the physical role of the disulfide bond.
Derives d'indole servant d'antagoniste de somatostatine
L'invention concerne un compose represente par la formule (I), dans laquelle le noyau A represente un noyau aromatique possedant eventuellement des substituants ; B, Y et Ya sont semblables ou


Platelet Aggregation Inhibitory Agents
This review covers the recent advances in the development of highly potent inhibitors of platelet aggregation as potential therapeutic drugs for thrombosis related to cardiovascular and
Antithrombotic agents: from RGD to peptide mimetics.
Conformationally constrained peptides and semipeptides derived from RGD as potent inhibitors of the platelet fibrinogen receptor and platelet aggregation.
The development of both 18 and 22 and the additional structural modifications within the constrained cyclic disulfide ring are described to probe the stereochemical and steric requirements for receptor interaction.
Investigation of conformational specificity at GPIIb/IIIa: evaluation of conformationally constrained RGD peptides.
NMR-based conformational analysis of an additional cyclic peptide, cyclo(Pro-Arg-Gly-Asp-D-Pro-Gy), is reported, and the conformational variations in the suite of peptides and related analogs are compared.
Low molecular weight, non-peptide fibrinogen receptor antagonists.
The tetrapeptide H-Arg-Gly-Asp-Ser-OH (1) (RGDS), representing a recognition sequence of fibrinogen for its platelet receptor GP IIb-IIIa (integrin alpha IIb beta 3), served as lead compound for the
Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
The ability of fibronectin to bind cells can be accounted for by the tetrapeptide L-arginyl-glycyl-L-aspartyl-L-serine, a sequence which is part of the cell attachment domain of fibronectin and