Adsorption of (Phe-h5)/(Phe-d5)-substituted peptides from neurotensin family on the nanostructured surfaces of Ag and Cu: SERS studies

Abstract

This work describes an application of Raman (RS) and surface-enhanced Raman scattering (SERS) to characterize the selective adsorption of two peptides belonging to the neurotensin family peptides, such as kinetensin (KN) and xenopsin-related peptide 2 (XP-2) that are known to stimulate the growth of human tumors. To perform a reliable analysis of SERS spectra, the L-Phe residue (at position 8 or 1 in the amino acid sequence of these peptides) was replaced with L-Phe-d₅ (five protons of L-phenylalanine ring substituted by deuterium). Native and (Phe-d₅)-isotopically labeled peptides were deposited on electrochemically nanostructured surfaces of Ag (AgORC) and Cu (CuORC) from an aqueous solution (H₂O). To determine the share of amide bonds in the interaction with the metallic substrate, SERS spectra of peptides adsorbed on AgORC from heavy water (D₂O) were measured. Also, to determine the effect of the C-end on the SERS spectrum, measurements were made for the KN analog in which the C-terminal L-leucine was removed ([desLeu⁹]KN). Based on the analyses of the spectral profiles, in the spectral range of 600-1650 cm^-1, specific conclusions have been drawn regarding specific aromatic ring···metal interactions and changes in the interaction during substrate change.

Keywords: Electrochemical nanostructured surfaces of silver (AgORC) and copper (CuORC); Isotopic substitution; Kinetensin, KN; Neurotensin-family peptides; Surface-enhanced Raman scattering, SERS; Xenopsin-related peptide 2, XP-2.