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- W2059690639 abstract "Two tripeptides, insulin-like growth factor I (IGF) (1−3) and gluthation (GSH), only differing by their central fragment, and one IGF-related dipeptide, Gly-Pro, were adsorbed on a Au(110) surface under UHV conditions. Studies of the kinetics of adsorption, as well as the chemical and structural characterization of the adlayers, were achieved by combining polarization modulation reflection absorption infrared spectroscopy and X-ray photoelectron spectroscopy techniques. Low-energy electron diffraction observations are also reported. The adsorption behavior varies drastically with the size and chemical composition of these three molecules. Gly-Pro, constituted of two of the three amino acids of IGF, adsorbs on the Au(110) surface, giving rise to a 2D organization and rapidly forming a full monolayer. The two tripeptides only differ by their central fragment and this modifies their growth mode drastically: IGF tends to form homogeneous, likely continuous, layers, while GSH adsorption results in heterogeneous layers with dimers or patches of molecules, leaving fractions of the gold surface bare or covered with a very thin layer of organics. Moreover, the average thickness of the IGF layer of on Au (110) increases faster than that of GSH with exposure time. The adsorption kinetics is faster for IGF than for GSH." @default.
- W2059690639 created "2016-06-24" @default.
- W2059690639 creator A5025995289 @default.
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- W2059690639 date "2009-05-01" @default.
- W2059690639 modified "2023-09-30" @default.
- W2059690639 title "Adsorption of Di- and Tripeptides on Au(110) under Ultrahigh Vacuum Conditions. 1. Polarization Modulation Reflection Absorption Infrared Spectroscopy and X-ray Photoelectron Spectroscopy Characterization" @default.
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- W2059690639 doi "https://doi.org/10.1021/jp9003888" @default.
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