L-cysteine, as an amino acid on the outer fringes of large proteins, can provide a link between those proteins and inorganic metal substrates. For the application of biomolecules (e.g., proteins) in electronic devices, it is essential to bond and organize the biomolecules on metals. L-cysteine presumably employs multiple functional groups (i.e., SH, NH2, and COOH) in its bonding to metal surfaces and anchors to the metal surface using either chemisorption (similar to thiolate-metal bonding) or physisorption (similar to the bonding to metal surfaces by the amino and carboxyl functional groups). These bonding strengths of L-cysteine, in particular the involvement of SH with the other functional groups, depend on the metallic partner properties. Therefore, an understanding of the interaction of L-cysteine with metal surfaces is necessary. Thus, in our previous studies, we have demonstrated different interaction strength and configurations of L-cysteine on the metallic surfaces of Au(111), Ag(111), and Cu(111) using ultraviolet photoemission spectroscopy (UPS) and in this study, the interface electronic structure of L-cysteine and Pd is systematically elucidated by UPS.
Kaveenga Rasika Koswattage
Dr. Kaveenga Rasika Koswattage (K.R. Koswattage) completed his PhD & MSc from Kobe University, Japan. He received his BSc special degree in Physics from University of Colombo. He worked as an assistant professor in Chiba University, Japan.Currently he is working as a senior lecturer in Sabaragamuwa University of Sri Lanka.
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LAP LAMBERT Academic Publishing
Amino Acids, photoemission spectroscopy, Electronic structure
SCIENCE / Physics