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International Journal of Spectroscopy
Volume 2012 (2012), Article ID 462901, 7 pages
Research Article

Protein Interactions Investigated by the Raman Spectroscopy for Biosensor Applications

1Laboratoire PEC, UMR CNRS 6087, Université du Maine, A.O. Messiaen, 72085 Le Mans, France
2Laboratoire de Chimie Organique, Université de Yaoundé I, B.P 812, Yaoundé, Cameroon
3Laboratoire UCO2M, UMR CNRS 6011, Université du Maine, A.O. Messiaen, 72085 Le Mans, France
4Laboratoire CBAC, UMR CNRS GEPEA 6144, IUT Université de Nantes, 85035 La Roche Sur Yon, France

Received 24 November 2011; Revised 27 January 2012; Accepted 10 February 2012

Academic Editor: Jaan Laane

Copyright © 2012 R. P. Kengne-Momo et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.