Interaction of cyclosporin A molecules with alkali and transition metal atoms on Cu(111).

The structure of a cyclic peptide with important biological functionalities, cyclosporin A (CsA), is investigated at the single molecule level. Its adsorption on Cu(111) under ultra-high vacuum is characterised with scanning tunnelling microscopy (STM) and density functional theory. With STM investigations, we demonstrate element specific on-surface coordination schemes of CsA with coadsorbed K, Co and Fe atoms. Thus, clear insights emerge in the behaviour of cyclic peptides at interfaces and their interactions with different metal atoms, providing control of the adsorption structure and assembly and paving the way for the integration of cyclic peptides in functional metal-organic nanostructures on surfaces.