Study Of The Interaction Between Bovine Serum Albumin And Salicylic Acid And Its Monohydroxy Substituted Derivatives

The study of interactions between proteins and ligand small molecules is a very common topic in the field of biochemistry.On the one hand,the study of the interaction between the two can provide a deeper understanding of the structure and function of biological proteins and facilitate further development and exploration of the use of proteins;on the other hand,the understanding of the interaction process between small molecules and proteins can further standardize the subsequent use of small molecules.Although some previous papers have studied the interaction process between bovine serum albumin(BSA)and other small molecules,the process only used steadystate fluorescence spectroscopy techniques to analyze the specific types of fluorescence quenching in combination with the changes of fluorescence intensity under different temperature conditions,and the conclusions were not sufficient.In this paper,for the interaction process between salicylic acid(SA)and its monohydroxy-substituted derivatives with bovine serum albumin(BSA),based on previous work,the following aspects were investigated:1.the fluorescence quenching process of BSA was investigated by means of steady-state fluorescence spectroscopy,time-resolved fluorescence spectroscopy and molecular docking techniques,and the types of fluorescence quenching of BSA after mixing with different small molecules were analyzed and determined.Combined with the results of molecular docking,it was determined that the fluorescence quenching was due to the energy transfer between BSA and SA and its monohydroxy substituted derivatives.The results contribute to a preliminary understanding and knowledge of the transport of small molecules in vivo and the metabolic processes.2.Combining the differences in the fluorescence quenching process of BSA with SA and its monohydroxy-substituted derivatives,and the differences in the distances between the donor and the acceptor obtained by molecular docking technique simulations,together with the results obtained by Circular Dichroism spectroscopy,an attempt was made to discuss and analyze the influence of structural differences of SA and its monohydroxy-substituted derivatives on their interactions with BSA.The results show that the number of hydroxyl groups and the substitution sites have different effects on the interaction process between small molecules and BSA.