L -Cysteine on Ag(111): A combined STM and X-ray spectroscopy study of anchorage and deprotonation

Sybille Fischer, Anthoula C. Papageorgiou, Matthias Marschall, Joachim Reichert, Katharina Diller, Florian Klappenberger, Francesco Allegretti, Alexei Nefedov, Christof Wöll, Johannes V. Barth

Research output: Contribution to journalArticlepeer-review

75 Scopus citations

Abstract

Thiols adsorbed on noble metals are prominent model systems for self-assembly and nanotechnology research. l-cysteine is the only proteinogenic amino acid containing a thiol group. A detailed knowledge of the interaction of this molecule with well-defined surfaces is essential to rationalize and advance interfacial amino acid self-assembly and the metal-mediated anchoring of proteins. Here, we address the exemplary system l-cysteine on Ag(111) in UHV, examined by direct STM observations, synchrotron-based XPS, and NEXAFS. Following adsorption, the molecules build up a dense-packed layer of zwitterions, attached to the surface via their sulfur atom. Upon annealing to 390 K, the cysteine molecules undergo pronounced chemical and conformational transformation, leading to a more complex assembly, driven by the deprotonation of the ammonium group.

Original languageEnglish
Pages (from-to)20356-20362
Number of pages7
JournalJournal of Physical Chemistry C
Volume116
Issue number38
DOIs
StatePublished - 27 Sep 2012

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