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Surface‐enhanced Raman scattering and theoretical studies of the C‐terminal peptide of the β‐subunit human chorionic gonadotropin without linked carbohydrates
Author(s) -
Aliaga A. E.,
Aguayo T.,
Garrido C.,
Clavijo E.,
Hevia E.,
GómezJeria J. S.,
Leyton P.,
CamposVallette M. M.,
SanchezCortes S.
Publication year - 2011
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21542
Subject(s) - chemistry , raman scattering , peptide , raman spectroscopy , amino acid , protein subunit , substrate (aquarium) , human chorionic gonadotropin , crystallography , biochemistry , optics , physics , oceanography , hormone , gene , geology
Abstract Raman and surface‐enhanced Raman scattering (SERS) spectra of the synthetic carboxy terminal peptide of human chorionic gonadatropin β‐subunit free of carbohydrate moieties (P37) are reported. The spectral analysis is performed on the basis of our reported Raman spectrum and SERS data of oligopeptides displaying selected amino acids sequences MRKDV, ADEDRDA, and LGRGISL. SERS samples of P37 were prepared by coating the solid peptide with metal colloids on a quartz slide. This treatment makes possible to obtain high spectral batch to batch reproducibility. Amino acids components of P37 display net charges and hydrophobic characteristics, which are related to particular structural aspects of the adsorbate–substrate interaction. The spectroscopic results are supported by quantum chemical calculations performed by using extended Hückel theory method for a model of P37 interacting with an Ag surface. The P37‐metal interaction is drove by positively charged fragments of selected amino acids, mainly threonine 109, lysine 122, and arginine in positions 114 and 133. Data here reported intend to contribute to the knowledge about the antigen–antibody interaction and to the drugs delivery research area. © 2010 Wiley Periodicals, Inc. Biopolymers 95: 135–143, 2011.