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Article Dans Une Revue International Journal of Spectroscopy Année : 2012

Protein Interactions Investigated by the Raman Spectroscopy for Biosensor Applications

Résumé

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.

Domaines

Matériaux
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Origine : Publication financée par une institution
Licence : CC BY - Paternité

Dates et versions

hal-02334802 , version 1 (25-08-2023)

Identifiants

Citer

R. Kengne-Momo, Ph. Daniel, Fabienne Lagarde, Y. Jeyachandran, J. Pilard, et al.. Protein Interactions Investigated by the Raman Spectroscopy for Biosensor Applications. International Journal of Spectroscopy, 2012, 2012, pp.1-7. ⟨10.1155/2012/462901⟩. ⟨hal-02334802⟩
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