Studies On The Interaction Of Drugs And Nanoparticles Materials With Bovine Serum Albumin By Spectroscopy

The research of drugs and nano-materials is very active in the life sciences,chemistry and clinical medicine topics. In vivo, serum albumin is an important carrierprotein, which can widely storage and transport lots of substances. Fluorescencespectrometry has been a concern and dependence analysis tool, because it has a highsensitivity, high selectivity, simple spectrum and prompt analysis, which is widely usedin biological macromolecules and drug small molecule. Similarly, with the rapid rise ofnano-materials, nano-materials occupied a large part of the field of scientific research,more and more people begin to take participate in researching it, and it is well used in thefield of biotechnology, which play a significant role for the progress of science. In thispaper, the interaction of drugs and nanomaterials with bovine serum albumin werestudied by the fluorescence spectroscopy, ultraviolet absorption spectroscopy andresonance light scattering. Moreover, the experiment could obtain the interaction of thequenching mechanism, binding force, binding distance and so on. It is deep-seated forunderstanding the mechanism of the serum albumin and small molecules, which canprovide useful information and data for life sciences research.In this thesis, the review involves the concept, development and characteristics ofdrug, nanomaterials and proteins, then summarize the interaction of the drugs andnano-materials with serum albumin of the research methods and the research progress inrecent years, as well as the interaction of drugs and nanoparticles materials with bovineserum albumin by spectral content. Finally, Finally, it is proposed that studies on theinteraction of the small molecules and nanomaterials with serum albumin has importantsignificance. The main contents are as follows: 1. In this paper, the interaction of mecobalamin with bovine serum albumin (BSA)was studied by fluorescence spectroscopy, resonance light scattering and ultravioletabsorption spectroscopy. It was shown that in pH7.40Tris-HCl buffer solution, both thefluorescence and resonance light scattering intensity of BSA were quenched by theincreasing of mecobalamin concentration, obviously. According to Stern-Volmer curveof the fluorescence quenching calculation, the quenching mechanism of mecobalaminwith BSA was a dynamic quenching. The binding constants, binding sites and thecorresponding thermodynamic parameters, namely enthalpy change (ΔH), free energychange (ΔG) and entropy change (ΔS) at different temperatures were calculated. From thethermodynamic parameters, the hydrophobic interactions was the main sort of bindingforce between the reaction of mecobalamin and BSA.2. The interaction between Ketotifen fumarate (KTF) and bovine serum albumin(BSA) was studied by fluorescence spectroscopy under the pH7.40Tris-HCl buffersystem. It was shown that the fluorescence intensity of bovine serum albumin could beapparently quenched by Ketotifen fumarate based on static quenching model. Theapparent binding constants (KA) and binding sites (n) were calculated at the differentsolution temperatures. Thermodynamic parameters (ΔH, ΔG and ΔS) for the KTF-BSAinteraction were measured, and it was proved that the major roles of binding force ofKTF-BSA was the hydrophobic. At the same time, the effect of the conformationbetween BSA and KTF was studied by the synchronous fluorescence spectroscopy. Inaddition, the mechanism of interaction of the KTF-BSA was studied by ultravioletabsorption spectrometry, which was agreed with the conclusions of the fluorescencespectrometry.3. The interaction between nanometer platinum (PtNP) and bovine serum albumin(BSA) was studied by fluorescence spectroscopy. It was show that PtNP caused thefluorescence quenching of BSA is a static quenching procedure. The binding constants(K≈104) and binding sites (n≈1) between PtNP and BSA were obtained, and according tothe values of thermodynamic functions, the type of force of PtNP and BSA was hydrophobic interactions. Meanwhile, The effect of PtNP on the conformation of BSAwas analysized by synchronous fluorescence. At last, the influence of the common ionMg2+, Zn2+and Fe3+to system of PtNP and BSA had also been studied, the resultsshowed that the ion Fe3+and PtNP have a competitive function to BSA.4. Under the pH7.40Tris-HCl buffer system, fluorescence spectroscopy was usedto investigate the influences of carbon nanotubes (CNTs) on the fluorescence ofamiodarone hydrochloride (AD) on bovine serum albumin(BSA) and the influences ofAD on that of BSA without CNTs. The experimental results demonstrated that AD couldquench the intrinsic fluorescence of BSA, and the quenching mechanism was dynamicquenching. The fluorescence quenching action of AD on BSA was strengthened in thepresence of CNTs. The binding constants KA, binding sites n and the correspondingthermodynamic parameters ΔH, ΔG and ΔS at different temperatures were calculated.Based on the thermodynamic parameters, it was proved that the major roles of bindingforce of AD-BSA was the electrostatic. The distance r of AD-BSA was evaluated.Moreover, the effect of AD on the conformation of BSA was studied by synchronousfluorescence spectroscopy. The results showed that AD changed the conformation of BSAduring the reaction. But the CNTs could not change the conformation of BSA. Thebinding constants KA, binding sites n of AD on BSA was increased in the presence ofCNTs. The discussion offered a reference study on the action mechanism of CNTs andAD with albumin in vivo.5. The interaction between cyproheptadine hydrochloride (CH) and bovine serumalbumin (BSA) in physiological solution was studied with and without coexisting Aunanoparticles (AuNP) by fluorescence spectroscopy. It was shown that the fluorescenceintensity of bovine serum albumin could be apparently quenched by cyproheptadinehydrochloride based on static quenching model. The apparent binding constants (KA) andbinding sites (n) were calculated at the different solution temperatures. Thermodynamicparameters (ΔH, ΔG and ΔS) for the CH-BSA interaction were measured, and it wasproved that the major roles of binding force of CH-BSA was the hydrophobic. The binding distance r is5.07nm and energy transfer efficiency E is0.0157. At the same time,the synchronous fluorescence spectroscopy was used to study the effect of CH on theconformation of BSA. In addition, the mechanism of interaction of the CH-BSA wasstudied by ultraviolet absorption spectrometry, which was agreed with the conclusions ofthe fluorescence spectrometry. Finally the effects of AuNP on the fluorescence of theCH-BSA interaction were evaluated.