A Study Of The Interaction Between Drugs Molecuales And Biomacromolecules

In this paper,the interaction between angiotensin converting enzyme inhibitors(such as fosinopril,benazapril,captopril and perindopril)and bovine serum albumin(BSA)and the interaction of sunitinib with DNA were investigated with the help of various spectroscopic methods and molecular docking.Combined the results of all spectroscopic and molecular docking,the more accurate and reliable conclusions were drawn as follows:First of all,with fluorescence emission spectroscopy we make further understand the quenching mechanism,binding site,number of binding site,binding constant of the interaction between angiotensin converting enzyme inhibitors and bovine serum albumin(BSA)under the simulated physiological conditions.Secondly,from the different binding constants under different temperatures,we get the thermodynamic constant and the binding force between BSA and ACEIs which is van der Waals force and hydrogen bonding interaction.What's more,the result of molecular docking approach had also reconfirmed these conclusions.In addition,UV spectroscopy,fourier transform infrared spectroscopy,synchronous fluorescence spectroscopy and 3D fluorescence spectroscopy proved that the conformation of BSA has been influenced because of binding with ACEIs.UV spectroscopy,fluorescence spectroscopy,circular dichroism(CD)and viscosity measurement had been used to investigate the interaction mode between sunitinib and DNA,which is groove binding.We also analyzed the binding site,number of binding site and binding constants under different temperatures with UV spectroscopy,and based on it to acquire the thermodynamic constant and the binding force which is hydrophobic interaction force and electrostatic force.All of results had been reconfirmed by molecular docking.