Docking of Novel Rgd Analogues with Αvβ3 Integrin

Ligand-protein interactions have been recognized as central phenomena in most biological processes ranging from catalysis to signaling . Theoretical and computational methods are widely used to analyze, investigate, and predict ligand-macromolecule interactions. In order to better understand the structural requirements of Integrins-ligand binding a series of RGD analogues were examined using docking techniques. The G-score of the DOTA (RGD-Nitrophe) is -9.09 which is the highest G-score value,-8.17 being the next highest score of RGD among all the ligand molecules.G-score of RGD-Nitrophe and [DTPA (Nitrophe-)2] is -7.35 and -7.49 simultaneously. Minimum energy is required for the more binding affinity of ligand and receptor complex. The E-value of DOTA (RGD-Nitrophe) is -114.83. DOTA (RGD-Nitrophe) required minimum energy for the formation of interaction complex which indicates DOTA (RGD-Nitrophe) have good binding affinity as compare to other RGD Analogs.