Underwater adhesion of mussel foot protein on a graphite surface

Abstract Mussel foot proteins (MFPs) strongly adhere to virtually any surfaces under wet conditions. This remarkable adhesion of MFP onto a hydrophilic surface could be attributed to the hydrogen bonds formed between MFP and surface. Little is known about the molecular origin of the underwater adhesion of MFP onto a nonpolar hydrophobic surface. By using all-atom molecular dynamics simulation, we investigate the structure, dynamics, and energy of the wet adhesion of a MFP onto a hydrophobic graphite. The MFP anchors on the graphite by directly contacting three L-3,4-dihydroxyphenylalanine (DOPA) groups. The present adhesion of MFP is even stronger than for a hydrophilic surface and arises from the van der Waals (π -π stacking) interaction between the phenylene rings of DOPAs and graphite.