Efficient immobilization of horseradish peroxidase enzyme on transition metal carbides

Abstract

In this study, the molecular dynamics simulation is performed to investigate the adsorption of horseradish peroxidase (HRP, a model enzyme) on Ti3C2 and Ti3C2OH (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 Ti3C2@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 Ti3C2 protects the conformation of enzymes more than Ti3C2OH. Hence, HRP can be effectually immobilized after the Ti3C2 in comparison to the Ti3C2OH. 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.