Spectroscopic Studies On The Interaction Of Drugs With Protein

Protein is the cornerstone of the human body.It takes the responsibility of making up all the cells and tissues in the human body.The study of protein is a core subject in the field of biomedicine.Among them,serum albumin has attracted much attention from biomedical researchers because of its own ability to combine drugs and carry them to the target.The study of the interaction between drugs and small molecules helps to understand the mechanism of drug delivery,distribution and entry into force,as well as the development and improvement of new drugs.Spectral analysis is a simple and effective way to study the interaction between drugs and proteins.Compared with other research methods,it has advantages of short operation time,easy operation,small sampling volume and high sensitivity.In this paper,the spectral characteristics of interaction between drugs and proteins were studied by fluorescence spectrometry,ultraviolet spectroscopy and synchronous fluorescence spectrometry combined with the equipment and instrument conditions in the laboratory.(1)The spectral quenching curves of the interaction between famotidine and bovine serum albumin were analyzed by fluorescence spectroscopy.The quenching types of bovine serum albumin were analyzed.By analyzing the change of the quenching curve at different temperatures,the binding constant and the number of binding sites of the drug and protein were further fitted,and the type of interaction was distinguished by thermodynamic constants.Finally,the distance between the intermolecular interactions was calculated by the nonradiative transfer theory.(2)The spectral characteristics of the interaction between metoprolol tartrate and bovine serum albumin were studied based on the spectroscopic method.The quenching type,the quenching constant and the proportion of the interaction between them were obtained by analyzing their fluorescence quenching spectra,And combined with the analysis of thermodynamic constants obtained the type of interaction between the two.(3)The interaction between mitiglinide and bovine serum albumin was studied by fluorescence spectroscopy and UV-Vis absorption spectroscopy.The relationship between the quenching type and the binding distance was calculated and analyzed.On the basis of this,the effect of mitiglinide calcium on the conformation of protein was analyzed by synchronous fluorescence spectroscopy.