1. Synthesis, biological evaluation, X-ray molecular structure and molecular docking studies of RGD mimetics containing 6-amino-2,3-dihydroisoindolin-1-one fragment as ligands of integrin αIIbβ₃.
- Author
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Krysko AA, Samoylenko GV, Polishchuk PG, Fonari MS, Kravtsov VCh, Andronati SA, Kabanova TA, Lipkowski J, Khristova TM, Kuz'min VE, Kabanov VM, Krysko OL, and Varnek AA
- Subjects
- Binding Sites, Biomimetic Materials metabolism, Biomimetic Materials pharmacology, Crystallography, X-Ray, Fibrinogen antagonists & inhibitors, Fibrinogen metabolism, Humans, Isoindoles metabolism, Isoindoles pharmacology, Ligands, Models, Molecular, Molecular Docking Simulation, Molecular Structure, Oligopeptides metabolism, Oligopeptides pharmacology, Phthalimides metabolism, Phthalimides pharmacology, Platelet Aggregation drug effects, Platelet Glycoprotein GPIIb-IIIa Complex antagonists & inhibitors, Platelet Glycoprotein GPIIb-IIIa Complex metabolism, Protein Binding, Biomimetic Materials chemistry, Isoindoles chemistry, Oligopeptides chemistry, Phthalimides chemistry, Platelet Glycoprotein GPIIb-IIIa Complex chemistry
- Abstract
A series of novel RGD mimetics containing phthalimidine fragment was designed and synthesized. Their antiaggregative activity determined by Born's method was shown to be due to inhibition of fibrinogen binding to αIIbβ₃. Molecular docking of RGD mimetics to αIIbβ₃ receptor showed the key interactions in this complex, and also some correlations have been observed between values of biological activity and docking scores. The single crystal X-ray data were obtained for five mimetics., (Copyright © 2013 The Authors. Published by Elsevier Ltd.. All rights reserved.)
- Published
- 2013
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