Enhanced selective immobilization of biomolecules onto solid supports coated with semifluorinated self-assembled monolayers.
A new strategy for the specific immobilization of proteins onto a solid support is presented. The immobilization is highly specific and efficient thanks to functionalized semifluorinated self-assembled monolayers (SAMs), thus reducing non-specific protein adsorption. Protein resistance does not exclusively result from classical steric repulsions and the presence of the both hydrophobic and lipophobic rigid and helical fluorinated cylinder in the depth of the SAMs does play an active role in protein repulsion. That repulsive effect is of higher magnitude than that of polyethylene glycol (PEG) as capping of the semifluorinated SAMs with additional ethylene oxide units provokes an attenuation of protein resistance. Though specific binding capacity of SAMs is intrinsically limited, the fluorinated SAMs described allow sensitive measurements with lower limits of detection and higher signal-to-noise ratios when compared to the best chips so far used in surface plasmon resonance (SPR) analysis.
Klein
Emmanuel
E
Laboratoire de Chimie Organique Appliquée, Faculté de Pharmacie, Institut Gilbert-Laustriat, UMR 7175-LC1, CNRS-Université Louis Pasteur, 74 Route du Rhin, BP 60024, 67401 Illkirch cedex, France.
Kerth
Paul
P
Lebeau
Luc
L
D001710:Biotin / Q000737:chemistry / Q000276:immunology; D017611:Fluorine Compounds / Q000138:chemical synthesis / Q000737:chemistry*; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology; D015394:Molecular Structure; D020349:Surface Plasmon Resonance; D013499:Surface Properties
D017611:Fluorine Compounds; D007074:Immunoglobulin G; D001710:Biotin