Lysozyme orientation and conformation on MoS₂ surface: Insights from molecular simulations

Area of Science:

• Materials Science
• Biophysics
• Nanotechnology

Background:

• Two-dimensional molybdenum disulfide (MoS2) exhibits unique properties, making it promising for biosensor applications.
• Understanding protein interactions with MoS2 is crucial for developing biocompatible platforms, but molecular-level details are lacking.

Purpose of the Study:

• To investigate the adsorption behavior of lysozyme protein on the MoS2 surface at the molecular level.
• To determine the preferred orientation and conformational changes of lysozyme upon adsorption.
• To identify the key interactions driving lysozyme adsorption on MoS2.

Main Methods:

• Molecular dynamics simulations were employed to study lysozyme adsorption.
• Six distinct lysozyme orientations were simulated based on its different faces.
• Analysis focused on adsorption orientation, conformational stability, and interaction forces.

Main Results:

• Lysozyme preferentially adsorbs onto the MoS2 surface in an "end-on" orientation (both "bottom end-on" and "top end-on").
• The adsorption process is primarily driven by van der Waals forces, with electrostatic interactions playing a supplementary role.
• The overall conformation of the lysozyme molecule was largely maintained after adsorption on the MoS2 surface.

Conclusions:

• The study provides fundamental insights into protein-MoS2 interactions, specifically for lysozyme.
• The findings indicate that end-on orientations are favorable for stable lysozyme adsorption on MoS2.
• This research can guide the design of MoS2-based biosensors and other biomedical applications.