Protein Interactions Investigated by the Raman Spectroscopy for Biosensor Applications

By R. P. Kengne-Momo, P. Daniel, F. Lagarde, Y. L. Jeyachandran, J. Pilard, Marie-José Durand-Thouand, G. Thouand. 2012

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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.

Subfields: Biophysics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/dc23bcef783d63b9bfd279c662c218a125c802ef