Surface Chirality of Gly-Pro Dipeptide Adsorbed on a Cu(110) Surface - Archive ouverte HAL
Article Dans Une Revue Chirality Année : 2015

Surface Chirality of Gly-Pro Dipeptide Adsorbed on a Cu(110) Surface

Résumé

The adsorption of chiral Gly-Pro dipeptide on Cu(110) has been characterized by combining in situ polarization modulation infrared reflection absorption spectroscopy (PM-RAIRS) and X-ray photoelectron spectroscopy (XPS). The chemical state of the dipeptide, and its anchoring points and adsorption geometry, were determined at various coverage values. Gly-Pro molecules are present on Cu(110) in their anionic form (NH2/COO-) and adsorb under a 3-point binding via both oxygen atoms of the carboxylate group and via the nitrogen atom of the amine group. Low-energy electron diffraction (LEED) and scanning tunneling microscopy (STM) have shown the presence of an extended 2D chiral array, sustained via intermolecular H-bonds interactions. Furthermore, due to the particular shape of the molecule, only one homochiral domain is formed, creating thus a truly chiral surface. Chirality 27:411-416, 2015. (c) 2015 Wiley Periodicals, Inc.

Dates et versions

hal-01238940 , version 1 (07-12-2015)

Identifiants

Citer

Hervé Cruguel, Christophe Méthivier, Claire-Marie Pradier, Vincent Humblot. Surface Chirality of Gly-Pro Dipeptide Adsorbed on a Cu(110) Surface. Chirality, 2015, 27 (7), pp.411-416. ⟨10.1002/chir.22445⟩. ⟨hal-01238940⟩
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