The
COVID-19 pandemic has claimed millions of lives worldwide,
sickened many more, and has resulted in severe socioeconomic consequences.
As society returns to normal, understanding the spread and persistence
of SARS CoV-2 on commonplace surfaces can help to mitigate future
outbreaks of coronaviruses and other pathogens. We hypothesize that
such an understanding can be aided by studying the binding and interaction
of viral proteins with nonbiological surfaces. Here, we propose a
methodology for investigating the adhesion of the SARS CoV-2 spike
glycoprotein on common inorganic surfaces such as aluminum, copper,
iron, silica, and ceria oxides as well as metallic gold. Quantitative
adhesion was obtained from the analysis of measured forces at the
nanoscale using an atomic force microscope operated under ambient
conditions. Without imposing further constraints on the measurement
conditions, our preliminary findings suggest that spike glycoproteins
interact with similar adhesion forces across the majority of the metal
oxides tested with the exception to gold, for which attraction forces
∼10 times stronger than all other materials studied were observed.
Ferritin, which was used as a reference protein, was found to exhibit
similar adhesion forces as SARS CoV-2 spike protein. This study results
show that glycoprotein adhesion forces for similar ambient humidity,
tip shape, and contact surface are nonspecific to the properties of
metal oxide surfaces, which are expected to be covered by a thin water
film. The findings suggest that under ambient conditions, glycoprotein
adhesion to metal oxides is primarily controlled by the water capillary
forces, and they depend on the surface tension of the liquid water.
We discuss further strategies warranted to decipher the intricate
nanoscale forces for improved quantification of the adhesion.