Study of the interaction mechanism between human serum albumin and Ti3C2Tx with different degrees of oxidation by multi-spectroscopic method and molecular docking

Currently, despite the wide application of Ti 3 C 2 T x in various fields, little information is available regarding its toxicity to humans, thus, it is necessary to study its interactions with human proteins as well as its biotoxicity. In the study, spectroscopic analysis and molecular simulation were used to investigated the interaction mechanism between human serum albumin (HSA) and Ti 3 C 2 T x with different oxidation degrees. The three prepared Ti 3 C 2 T x materials with different oxidation degrees were analyzed by X-ray diffractometer, X-ray photoelectron spectroscopy, scanning electron microscope and transmission electron microscope, and the results demonstrated that TiO 2 nanoparticles were formed during the oxidation process. In conclusion, the results of the ultra violet spectrum, fluorescence spectra and zeta potential measurements showed that fully oxidized Ti 3 C 2 T x (F-Ti 3 C 2 T x ) had a greater binding ability to HSA than unoxidized Ti 3 C 2 T x (U-Ti 3 C 2 T x ), followed by partially oxidized Ti 3 C 2 T x (P-Ti 3 C 2 T x ). Based on synchronous fluorescence, circular dichroism and infrared characterization, it has been determined that with a gradual increase of Ti 3 C 2 T x oxidation degree, its effect on the conformation of HSA increases, followed by F-Ti 3 C 2 T x > P - Ti 3 C 2 T x > U - Ti 3 C 2 T x . Further analysis of the fluorescence binding ability revealed that hydrogen bonds played a major role in the interaction between HSA and Ti 3 C 2 T x .