SARS-CoV-2 proteins show great binding affinity to resin composite monomers and polymerized chains.

Abstract

Background: Due to saliva and salivary glands are reservoir to severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2), aerosols and saliva droplets are primary sources of cross-infection and are responsible for the high human-human transmission of SARS-CoV-2. However, there is no evidence about how SARS-CoV-2 interacts with oral structures, particularly resin composites.

Aim: To evaluate the interaction of SARS-CoV-2 proteins with monomers present in resin composites using in silico analysis.

Methods: Four SARS-CoV-2 proteins [i.e. main protease, 3C-like protease, papain-like protease (PLpro), and glycoprotein spike] were selected along with salivary amylase as the positive control, and their binding affinity with bisphenol-A glycol dimethacrylate, bisphenol-A ethoxylated dimethacrylate, triethylene glycol dimethacrylate, and urethane dimethacrylate was evaluated. Molecular docking was performed using AutoDock Vina and visualised in Chimera UCSF 1.14. The best ligand-protein model was identified based on the binding energy (ΔG-kcal/moL).

Results: Values for the binding energies ranged from -3.6 kcal/moL to -7.3 kcal/moL. The 3-monomer chain had the lowest binding energy (i.e. highest affinity) to PLpro and the glycoprotein spike. Non-polymerised monomers and polymerised chains interacted with SARS-CoV-2 proteins via hydrogen bonds and hydrophobic interactions. Those findings suggest an interaction between SARS-CoV-2 proteins and resin composites.

Conclusion: SARS-CoV-2 proteins show affinity to non-polymerised and polymerised resin composite chains.