Multidentate binding of two helical hexapeptides to a gold surface wasobtained by introducing in the peptide chain a non ribosomial amino acid, i.e. the 4-amino-1,2-dithiolane-4-carboxylic acid (Adt) residue, a C!-tetrasubstituted !- amino acid bearing a heterocyclic side chain characterized by a disulfide group. The two peptides, mainly formed by strongly helicogenic C!-tetrasubstituted !- amino acids, were both functionalized at the N-terminus by a ferrocenoyl (Fc) group, but differ in the number of Adt residues included in the peptide chain: the former (Fc6Adt2) contains two Adt residues at positions 1 and 4, while its analog (Fc6Adt1) contains a single Adt at position 4, since the Adt at position 1 is substituted by an !-amino isobutyric acid (Aib) residue. This peptide design allowed us to explore the different electrochemical properties and morphologies shown by the two peptide layers immobilized on a gold surface by two (Fc6Adt2) or a single (Fc6Adt1) bidentate linker, respectively. The electrochemical activity of the ferrocenoyl probe embedded in the peptide film was characterized by cyclic voltammetry, chronoamperometry and square wave voltammetry, while the binding and themorphology of the peptide layerswere studied by X-ray photoelectron spectroscopy (XPS) and ultra high vacuum scanning tunneling microscopy (UHVSTM), respectively. Significant differences were observed in the electron transfer (ET) properties of the two peptides investigated, which emerge from the diverging morphology achieved by the peptide layers on the gold surface. It was found that while a standing-up configuration of the peptide layer, realized by a single bidentate linkage, maximizes the ET efficiency, a lying down configuration (two Adt linkages) allows for precise positioning of Fc in the proximity of a gold surface.

Caruso, M., Gatto, E., Palleschi, A., Scarselli, M.a., DE CRESCENZI, M., Formaggio, F., et al. (2016). Are two better than one? A new approach for multidentate grafting of peptides to a gold substrate. ZEITSCHRIFT FÜR PHYSIKALISCHE CHEMIE, 230(9), 1351-1371 [10.1515/zpch-2015-0729].

Are two better than one? A new approach for multidentate grafting of peptides to a gold substrate

CARUSO, MARIO;GATTO, EMANUELA;PALLESCHI, ANTONIO;SCARSELLI, MANUELA ANGELA;DE CRESCENZI, MAURIZIO;VENANZI, MARIANO
2016-01-01

Abstract

Multidentate binding of two helical hexapeptides to a gold surface wasobtained by introducing in the peptide chain a non ribosomial amino acid, i.e. the 4-amino-1,2-dithiolane-4-carboxylic acid (Adt) residue, a C!-tetrasubstituted !- amino acid bearing a heterocyclic side chain characterized by a disulfide group. The two peptides, mainly formed by strongly helicogenic C!-tetrasubstituted !- amino acids, were both functionalized at the N-terminus by a ferrocenoyl (Fc) group, but differ in the number of Adt residues included in the peptide chain: the former (Fc6Adt2) contains two Adt residues at positions 1 and 4, while its analog (Fc6Adt1) contains a single Adt at position 4, since the Adt at position 1 is substituted by an !-amino isobutyric acid (Aib) residue. This peptide design allowed us to explore the different electrochemical properties and morphologies shown by the two peptide layers immobilized on a gold surface by two (Fc6Adt2) or a single (Fc6Adt1) bidentate linker, respectively. The electrochemical activity of the ferrocenoyl probe embedded in the peptide film was characterized by cyclic voltammetry, chronoamperometry and square wave voltammetry, while the binding and themorphology of the peptide layerswere studied by X-ray photoelectron spectroscopy (XPS) and ultra high vacuum scanning tunneling microscopy (UHVSTM), respectively. Significant differences were observed in the electron transfer (ET) properties of the two peptides investigated, which emerge from the diverging morphology achieved by the peptide layers on the gold surface. It was found that while a standing-up configuration of the peptide layer, realized by a single bidentate linkage, maximizes the ET efficiency, a lying down configuration (two Adt linkages) allows for precise positioning of Fc in the proximity of a gold surface.
2016
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore CHIM/02 - CHIMICA FISICA
Settore FIS/03 - FISICA DELLA MATERIA
English
Con Impact Factor ISI
4-Amino-1,2-dithiolane-4-carboxylic acid (Adt), Ferrocenoyl-Peptide Conjugates, Peptide Foldamers, PeptideMaterials, Peptide Self-Assembled Monolayers.
Caruso, M., Gatto, E., Palleschi, A., Scarselli, M.a., DE CRESCENZI, M., Formaggio, F., et al. (2016). Are two better than one? A new approach for multidentate grafting of peptides to a gold substrate. ZEITSCHRIFT FÜR PHYSIKALISCHE CHEMIE, 230(9), 1351-1371 [10.1515/zpch-2015-0729].
Caruso, M; Gatto, E; Palleschi, A; Scarselli, Ma; DE CRESCENZI, M; Formaggio, F; Longo, E; Toniolo, C; Wright, K; Venanzi, M
Articolo su rivista
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/176301
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