Probing SARS-CoV-2 Membrane Binding Peptide via Single-Molecule AFM-based Force Spectroscopy

The files provided here contain the raw Atomic Force Microscopy (AFM) data underlying the force measurements recorded in our study on SARS-CoV-2 spike protein membrane interactions. This study, titled “The SARS-CoV-2 spike protein’s membrane-binding domain bridges the viral and host cell membrane, a critical step in triggering membrane fusion,” investigates the binding dynamics of the SARS-CoV-2 spike protein with host cell membranes. Specifically, we focused on a membrane-binding peptide (MBP) near the TMPRSS2 cleavage site, examining both primed (TMPRSS2-cleaved) and unprimed states, as well as the effects of a conserved disulfide bridge on membrane stability and binding affinity. The data presented here are crucial in demonstrating the MBP’s preferential association with cholesterol-rich membranes and the stabilizing role of the disulfide bridge in membrane interactions.