A simple method of surface functionalisation for immuno-specific immobilisation of proteins.
We present a new and advanced methodology, developed for surface functionalisation of gold and to study immobilisation of an immuno-specific system of proteins. A combination of electrochemical quartz crystal microbalance and Raman spectroscopy techniques allowed a complete understanding of the system starting from surface functionalisation and progressing to the functional structure analysis of immobilised proteins. A simple electrochemical procedure was formulated to prepare sulphonyl chloride terminated gold surfaces that form a strong sulphonamide bond with the receptor protein staphylococcal protein A (SpA). On the SpA grafted surfaces, the immobilisation of a human IgG and consecutive binding of an immuno-specific anti-human IgG was observed. The surface functional groups form a strong interaction with SpA without disturbing its functional properties. The native functional structure of SpA and also the IgGs was found to be retained in their immobilised state.
Kengne-Momo
R P
RP
Laboratoire PEC, UMR CNRS 6087, Université du Maine, A.O. Messiaen, 72085, Le Mans, France.
Jeyachandran
Y L
YL
Assaf
A
A
Esnault
C
C
Daniel
P
P
Pilard
J F
JF
Durand
M J
MJ
Lagarde
F
F
Dongo
E
E
Thouand
G
G
D004563:Electrochemistry; D007074:Immunoglobulin G / Q000737:chemistry; D013059:Spectrum Analysis, Raman; D013205:Staphylococcal Protein A / Q000737:chemistry*
D007074:Immunoglobulin G; D013205:Staphylococcal Protein A