Author(s): Feyer V, Plekan O, Tsud N, Chb V, Matoln V,
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Abstract The adsorption of histidine (His) and three His-derived peptides on Au(111) has been studied by soft X-ray photoelectron spectroscopy (XPS) and near-edge X-ray absorption fine structure spectroscopy (NEXAFS) at the nitrogen and oxygen K edges. The peptides were glycyl-histidine (Gly-His), glycyl-histidine-glycine (Gly-His-Gly), and glycyl-glycyl-histidine (Gly-Gly-His) and were adsorbed at saturated coverage on the Au(111) surface from aqueous solution. Coverages of 1 and 0.5 monolayers (ML) of His were adsorbed by evaporation in vacuum and compared with 1 ML deposited from solution. There were no significant chemical differences between the monolayers deposited in vacuum or from solution. The Au 4f core level shift indicates that a chemisorption rather than a physisorption bond is formed. In both deposited phases, His bonds to the gold surface in anionic form via the imino nitrogen atom of the imidazole ring and the oxygen atoms of the carboxylate group. N and O K-edge NEXAFS indicate that the ring and carboxylate triangle of adsorbed His are tilted at approximately 35 degrees and approximately 27 degrees, respectively, with respect to the Au(111) surface. The peptides bond to the gold surface in a mode similar to the single His molecule, via the imino and carboxylate groups, while the peptide group is at a steep angle to the surface. However, the peptides adsorb with a higher atomic density, consistent with the peptide groups being above the surface. There are also differences between Gly-His-Gly and Gly-Gly-His, implying that the sequence within the peptide has a significant influence on the bonding geometry.
This article was published in Langmuir
and referenced in Journal of Steel Structures & Construction