Comparative analysis of interactions between the hydropyridine dicarboxylate derivatives and different proteins by molecular docking and charge density analysis

摘要: Molecular docking and charge density analysis were carried out to understand the geometry, distribution electrostatic properties of one newly synthesized 4-substituted-2,6-dimethyl-1,4-dihydropyridine-3,5-dicarboxylates (PDE), which is regarded as best α-Glucosidase inhibitor among hydropyridine dicarboxylate derivatives. The different bonding models PDE molecule in active sites proteins Human serum albumin (HSA) Saccharomyces cerevisiae α-glucosidase (SAG) are firstly compared, important intermolecular interactions between drug-transport protein drug-target protein. deformation maps suggest that electron densities redistributed when it presents sites. When site SAG, evident find negative region does not appear at vicinity oxygen atoms on carboxylic acid dimethyl ester group. Frontier molecular orbital distributions for similar all forms. highest occupied (HOMO) lowest (LUMO) energy gaps higher than pure solution phase. It generally noticed orientations dipole moment vectors reoriented both These fine details electronic level allow better exact interactions.