The adsorptions of tryptophan (Trp) on silver or gold surfaces were investigated by surface-enhanced Raman scattering (SERS) measurements. In addition, peptides with Trp in different chain positions were studied and the adsorption sites were determined based on marker bands. The indole ring was the main group responsible for the interactions with gold nanoparticles (AuNPs). In the presence of HCl, the SERS spectra suggested that the anchoring of such peptides on AuNPs was reinforced by ionic pair interactions between protonated amine and chloride ions. The adsorptions of Trp and its derivatives on silver nanoparticles (AgNPs) show some variability in the spectral patterns, even though the enhanced carboxilate and amino features were ever ascribed as preferable adsorption site. Based on DFT calculations the vibrational assignment allows the reinterpretation of previous published works. The investigations showed that both the high affinity of indole moiety for the AuNP surfaces make these substrates adequate for studying the adsorption of peptides containing Trp and the proposed SERS assignments could be helpful for further studies of more complex structures.
Keywords: Adsorption geometry; Oligopeptide; Protein; Surface chemistry; Vibration spectroscopy.
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