Probing of Interaction between Alogliptin Benzoate and Human Serum Albumin Using Multi-Spectral Methods and Molecule Docking Technique

The interaction of alogliptin benzoate with human serum albumin had been characterized under physiological conditions using multi-spectral methods and molecular docking technique. The work presented in this paper focused on the interaction mechanism, the conformational changes of HSA and the binding sites of alogliptin benzoate with human serum albumin. The binding distance, binding constants, the number of binding sites and the binding forces had been investigated through fluorescence and spectral overlaps. Results indicated the presence of static quenching between alogliptin benzoate and human serum albumin. Moreover, the van der Waals forces and hydrogen bonding drove the binding process. The analysis results of UV–vis absorption spectroscopy, synchronous fluorescence spectrometry, circular dichroism spectroscopy and three-dimensional fluorescence spectroscopy revealed that alogliptin benzoate changed the conformation of human serum albumin. In addition, molecule docking and competitive experimental results suggested the binding sites located at IIA subdomain of human serum albumin. This research is vital to providing reference for studying the pharmacodynamics and pharmacokinetics mechanisms of alogliptin benzoate.