Coronaviruses are known for their distinctive spike glycoprotein (S-protein) protruding from viral particles. An all-atom molecular dynamics simulations was conducted to explore how the S-protein interacts with a polylactic acid surface at three temperatures: 3°C representing the food cold chain, 24°C corresponding to typical room conditions, and 50°C signifying extreme heat.

The findings show that Van der Waals and hydrogen bonding drove S-protein adsorption onto PLA, especially with arginine and lysine amino acids, which contributed the greatest to binding energy. The strongest interaction occurred at 24°C, possibly due to PLA properties. Conversely, interactions with PLA were weaker at 3°C and 50°C, marked by smaller van der Waals interactions near N-terminal and receptor-binding domain residues. S-protein was most stable at 3°C, somewhat less at 24°C, and highly unstable at 50°C.

The results suggest that SARS-CoV-2 virions can strongly adhere to PLA surfaces at room temperature, posing potential infection risks. Therefore, extra precautions may be necessary in environments where PLA is used at this temperature, such as medical facilities employing PLA-based PPE or supermarkets packaging food in PLA materials, to ensure effective virus disinfection.

The snapshots of each complex system (T = 3, 24 and 50 Celsius degrees) at three different time points (t = 0, 1 and 2μs) from the x front perspective.

Graphical depiction of computational methodology.

Karin Hasegawa

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