Unravelling the GLY-PRO-GLU tripeptide induced reconstruction of the Au(110) surface at the molecular scale.

Highlights • The adsorption of GLY-PRO-GLU tripeptide on Au(110) is investigated using FF-MD and DFT. • GLY-PRO-GLU adsorption reorganizes and restructures the Au(110) surface. • A mechanism for the surface restructuration is proposed at room temperature in UHV. • The glutamic acid residue is found to be responsible for the surface reconstruction. Abstract The adsorption of GLY-PRO-GLU tripeptide on Au(110) is investigated within the frame of all atom classical mechanics simulations and Density Functional Theory, focusing on the surface reconstruction. It is shown that the tripeptide adsorption reorganizes and restructures the Au(110) surface. A mechanism for the surface restructuration is proposed for both the neutral and zwitterionic form of the peptide at room temperature in Ultra High Vacuum. Diverse residues may be involved in the Au atoms displacement, and in particular glutamic acid, triggering a double proton transfer and the formation of a zwitter ionic state, is found to be responsible for the triggering of the surface reconstruction. Graphical abstract Image, graphical abstract [ABSTRACT FROM AUTHOR]