Open AccessProtein Interactions Investigated by the Raman Spectroscopy for Biosensor Applications
Author(s) -
R. P. Kengne-Momo,
Philippe Daniel,
Fabienne Lagarde,
Y.L. Jeyachandran,
J.F. PILARD,
Marie-José Durand-Thouand,
Gérald Thouand
Publication year - 2012
Publication title -
international journal of spectroscopy
Language(s) - English
Resource type - Journals
eISSN - 1687-9457
pISSN - 1687-9449
DOI - 10.1155/2012/462901
Subject(s) - raman spectroscopy , biosensor , chemistry , tyrosine , amino acid , protein–protein interaction , helix (gastropod) , protein structure , biophysics , protein a , immunoglobulin g , biochemistry , crystallography , antibody , biology , physics , immunology , ecology , snail , optics
Interaction and surface binding characteristics of staphylococcal protein A (SpA) and an anti-Escherichia coli immunoglobulin G (IgG) were studied using the Raman spectroscopy. The tyrosine amino acid residues present in the α-helix structure of SpA were found to be involved in interaction with IgG. In bulk interaction condition the native structure of proteins was almost preserved where interaction-related changes were observed in the overall secondary structure (α-helix) of SpA. In the adsorbed state, the protein structure was largely modified, which allowed the identification of tyrosine amino acids involved in SpA and IgG interaction. This study constitutes a direct Raman spectroscopic investigation of SpA and IgG (receptor-antibody) interaction mechanism in the goal of a future biosensor application for detection of pathogenic microorganisms
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