Efficient immobilization of horseradish peroxidase enzyme on transition metal carbides.

• HPX im5mobilization on Ti 3 C 2 and Ti 3 C 2 OH surfaces is explored by the MD simulation method. • It has been found that and van der Waals and electrostatic interactions regulate enzyme immobilization. • During absorption process, the HPX composition remains unchanged, indicating the excellent biocompatibility of Ti 3 C 2 and Ti 3 C 2 OH. • The MD simulation results illustrated that the structure of the HPX is more protected on the Ti 3 C 2 surface. In this study, the molecular dynamics simulation is performed to investigate the adsorption of horseradish peroxidase (HRP, a model enzyme) on Ti 3 C 2 and Ti 3 C 2 OH (as templates for enzyme immobilization). It has been found that van der Waals and electrostatic interactions regulate enzyme immobilization, whereas the hydrogen bonding between enzyme and MXene is involved in the adsorption process. The simulation outcomes indicate that various MXene can effectually adsorb HRP, and the adsorption strength is more for the Ti 3 C 2 @HRP complex, as revealed by energy analysis (interaction energy = −710.92 vs −449.02 kJ mol−1). Moreover, the root means square deviation, root means square fluctuation and secondary structure analysis indicate that Ti 3 C 2 protects the conformation of enzymes more than Ti 3 C 2 OH. Hence, HRP can be effectually immobilized after the Ti 3 C 2 in comparison to the Ti 3 C 2 OH. In the following, the evaluation of 2-thiouracil (2-Thi) ability to modulate HRP activity is investigated. The obtained results show that 2-Thi inhibitor has a great capacity to inhibit HRP enzyme. Eventually, the stability of immobilized HRP at higher temperatures (330 and 363 K) and acidic pH is examined. The present work suggests theoretical insights into realizing the biocompatibility of MXenes and instructs for modeling efficacious synthetic inhibitors. [ABSTRACT FROM AUTHOR]