Research On The Interaction Of Drugs And Biomolecules By Spectroscopic Methods

Protein is an important component of all living organisms, plays a special role in the organismsand is the material basis of living body. The binding of protein to drug has a great effect upon thedistribution of drugs in the body, upon their patterns of metabolism and excretion. Hypertension is themost commom chronic disease in many countries, which is an important risk factor caused the heart,cerebrovascular and renal disease. In the recent years, its incidence has been rising and has become aworrying important issue. Therefore, it is an urgent task to study its distribution in the body, bindingaction and how to use drugs rationally.This work has been carried out under the above-mentioned background and carries out to aseries studies on the basis of laboratory. This paper mainly studies the interaction betweenanti-hypertension drugs and protein by spectroscopic technology. The results could not only helpfulfor understanding the binding constants, the number of binding sites and conformational changes ofprotein affected by drugs, but also provide useful technical support for appropriately understandingthe drug’s toxicity, design and development of new drugs.(1) The binding mechanism of several kinds of hypertension drugs to bovine serum albumin(BSA) were studied by fluorescence, UV-vis, time-resolved fluorescence and Resonance LightScattering (RLS) spectroscopy. The binding properties including the fluorescence quenchingmechanisms, binding constants, binding distance and the number of binding sites were obtained. Theresults show that drug cause the fluorescence quenching of BSA through a static quenching procedure.The results of thermodynamic parameters show that the binding of drug to BSA is a spontaneousprocess and the interaction between drug and BSA is driven mainly by hydrophobic forces. Thesemay provide scientific basis for understanding the drug’s efficacy of the detailed process, scientificand rational drug use and drug design and development.(2) The effects of drug on BSA second structure were investigated based on synchronousfluorescence, FT-IR and three-dimensional fluorescence spectroscopy techniques. The changed valuesof the content of the secondary structure of BSA interacts before and after drug were obtained, whichextends the content to study the system of interaction between BSA and drug. These may providescientific basis for further exploring the binding mechanism of the drug to BSA.(3) The interaction between bovine serum albumin and drug (troxerutin) was further studied bysynchronous fluorescence spectroscopy and multivariate curve resolution-alternating least squares method. The number of species, pure spectra for each species and concentration profiles wereobtained, which further confirmed the information of the binding drug to BSA by fluorescencespectroscopy.(4) The spectral characteristics of the interaction between drugs and human serum were studiedby spectral method in body temperature. With the same excitation light, the fluorescence intensitydecrease with the increasing drug concentration when the interaction between human serum and thedifferent concentration drug, and the best excitation wavelength is at290nm. The absorption spectraof human serum interacts drug before and after have taken place significant changes, mainly in theabsorption peak position and absorbance intensity. Investigating the spectral characteristics ofinteraction between human serum and drug could help to understand the information of theirinteractions and provide a valuable reference for clinical medicine and development of appropriatemedical devices.