Binding interactions of MoS2 quantum dots with hemoglobin and their adsorption isotherms and kinetics in vitro

Abstract

To elucidate the binding interaction and adsorption isotherms and kinetics of molybdenum disulfides quantum dots (MoS2 QDs) with bovine hemoglobin (BHB) in vitro, it is urgent to investigate their binding mechanism in this work. The experimental results indicated that MoS2 QDs partly induced denaturation and expansion of secondary structure of BHB and the microenvironment changes of heme by the ground state complex formation of BHB with MoS2 QDs. The tertiary structure and the thermal denaturation of BHB on MoS2 QDs surface are not obviously different from only BHB solution. The experimental results were verified correctness with molecular modeling analysis. The Soret band changes indicated that the presence of MoS2 QDs partly protects the oxidation process of BHB by H2O2. In addition, the kinetics of BHB adsorption onto MoS2 QDs follows the pseudo-second-order kinetic model with high adsorption capacity, their adsorption was a fast process. This in vitro study could act as a precedent in understanding the interaction mechanism of biomolecules with MoS2-based nanomaterials.