Study On Interaction Of Protein With Small Molecule Drugs

Protein is one of the important organic material in humans andanimals, which perform complex biological functions. So protein is wellknown as “functional macromolecules”. Protein funtion can be identified bymany important phenomena of life and physical activities, in other words, alllife phenomena are the function of the protein. The researching field of theprotein is an important project in many researching area such as chemistry,life sciences, medical science and so on.. Especially for the research of theinteraction between protein and small molecule drugs, such as building vitromodel of the protein–drug system, understanding the combination of closedegree, combining site, binding force, and binding constant and so on, whichnot only contribute to the role of protein and small molecule mechanism andregularity in the molecular level, learning the relationship between proteinstructure and function, providing useful information for life science researchand data, but also for our understanding of the transportation and distributionof drug in the body, drug toxicity and new drug design and developmnet,which have very important guiding significance.The major works are researched as follows:1.The interaction between bovine serum albumin (BSA) and rutin has beeninvestigated in vitro under a simulated physiological condition by UV-Visspectrophotometry, fluorescence spectrometry and cyclic voltammetry. Thebinding constants of3.2×106L/mol and5.3×106L/mol can be calculated fromthe data obtained from fluorescence quenching experiments and cyclicvoltammetry, respectively. And the number of the binding sites is nearly1.5.The observations are rationalized in terms of a static quenching process atlower concentrations of rutin and a combined quenching (both dynamic andstatic) process at higher concentrations of rutin. Within the limits, thefluorescence intensity changes of BSA linearly with the concentrations ofrutin, the linear range is between8.00×10-8and1.00×10-5mol/L, and the detection limit is7.00×10-8mol/L. Within the limits, the redox peak current ofrutin was proportional to the the concentration of BSA, the linear range isbetween7.00×10-9and1.00×10-6mol/L, and the detection limit is5.00×10-9mol/L. It has been applied to the determination between BSA and rutin withsatisfactory results.2. The interaction between taxifolin and bovine serum albumin(BSA) wasinvestigated using UV/Vis, fluorescence and. cyclic voltammetry. The bindingconstants of1.3×106L/mol and1.6×106L/mol can be calculated from the dataobtained from fluorescence quenching experiments and cyclic voltammetry,respectively. And the number of the binding sites is nearly1.3. The interactionof bovine serum albumin with taxifolin was a single static quenchingprocedure. Within the limits, the fluorescence intensity changes of BSAlinearly with the concentrations of taxifolin, the linear range is6.00×10-7~2.00×10-5mol/L, and the detection limit is2.00×10-7mol/L. Withinthe limits, the redox peak current of taxifolin was proportional to the theconcentration of BSA, the linear range is7.00×10-7~1.00×10-4mol/L, and thedetection limit is3.00×10-7mol/L. It has been applied to the determinationbetween BSA and taxifolin with satisfactory results.