Synthesis of 2-aminonaphthalene-1-sulfonic acid Schiff bases and their interactions with human serum albumin

Abstract

Abstract Objectives Human serum albumin (HSA) can bind and transport many substances to cells to meet various needs of the organism. The binding efficacy of HSA to these substances directly affects their functions. In this paper two Schiff base compounds were synthesized to explore the interaction between HSA and both compounds. Methods Fluorescence spectra and an AutoDock model were utilized to investigate the interaction mechanism and binding model between proteins and Schiff base products. The conformation change of HSA was detected by resonance light scattering and circular dichroism spectra. Results The two compounds bound easily with HSA, with binding constants of 104. The binding sites for both compounds in HSA were within an appropriate distance for long-range interactions. Both compounds are accommodated in hydrophobic domains of HSA. However, electrostatic interactions and other supermolecular forces coexist between the compounds and protein. Binding of these compounds disturbed the protein secondary structure and caused a certain degree of destabilization. Conclusions The two Schiff base compounds can interact with HSA with high efficacy, which is helpful for explore the application of this type of Schiff base in biomedical research.