Synthesis, biological evaluation and molecular docking studies of 2-piperazin-1-yl-quinazolines as platelet aggregation inhibitors and ligands of integrin αIIbβ3

Bioorg Med Chem Lett. 2016 Apr 1;26(7):1839-43. doi: 10.1016/j.bmcl.2016.02.011. Epub 2016 Feb 22.

Abstract

A series of 2-piperazin-1-yl-quinazolines were synthesized and evaluated for their antiaggregative activity. The synthesized small molecule compounds have potently inhibited platelet aggregation in vitro and blocked FITC-Fg binding to αIIbβ3 integrin in a suspension of washed human platelets. The key αIIbβ3 protein-ligand interactions were determined in docking experiments and some correlations have been observed between values of the affinity and docking scores.

Keywords: 2-Piperazin-1-yl-quinazoline; Fibrinogen receptor antagonists; Platelet aggregation; α(IIb)β(3).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blood Platelets / cytology
  • Blood Platelets / drug effects*
  • Blood Platelets / metabolism
  • Humans
  • Ligands
  • Molecular Docking Simulation
  • Piperazines / chemistry
  • Piperazines / pharmacology
  • Platelet Aggregation / drug effects
  • Platelet Aggregation Inhibitors / chemistry*
  • Platelet Aggregation Inhibitors / pharmacology*
  • Platelet Glycoprotein GPIIb-IIIa Complex / metabolism*
  • Quinazolines / chemistry*
  • Quinazolines / pharmacology*

Substances

  • Ligands
  • Piperazines
  • Platelet Aggregation Inhibitors
  • Platelet Glycoprotein GPIIb-IIIa Complex
  • Quinazolines