Recognition antibody/antigen

Webster, D. M. Rees, A. R. (1993). Macromolecular recognition antibody-antigen complexes. Prot Eng 65, 94. 

Colman, P.M. Structure of antibody-antigen complexes implications for immune recognition. Adv. Immunol. 43 99-132, 1988. 

The tuneable nature of the evanescent field penetration depth is critical to the effective operation of this sensor as it facilitates surface-specific excitation of fluorescence. This means that only those fluorophores attached to the surface via the antibody-antigen-labelled antibody recognition event... 

The Agilent multiple affinity removal system utilizes the specificity of antibody-antigen recognition for 14 highly abundant proteins from human serum samples. The affinity column achieves reproducible and specific depletion from human serum and plasma to eliminate 94% of interfering proteins. It allows identification of proteins down to nanograms per milliliter level as reported by Agilent. 

Determining the thermodynamics and kinetics of recognition between biomolecules, particularly when one of the two is immobilized on a substrate, is of considerable current interest, as for example, antibody-antigen recognition, recognition of single-stranded DNA oligonucleotides by partially or totally complementary DNA strands, and many other possible analytical applications. 

In fields such as biosensing, analyte binding often relies on very specific molecular recognition interactions that nature has supplied, such as antibody-antigen interactions or strands of complimentary DNA forming double hefices. Unfortunately, because versatile and highly selective receptors for TNT or other explosive molecules are not available, chemists are left to rely on less specific interactions. 

Specific, rapid, and high-affinity recognition of antigens by antibodies is essential for the host s immune system to respond to invasion by foreign cells and pathogens. Pecht and Lancet have presented a cogent analysis of antibody interactions with haptens, and the interested reader will find their examination of the kinetics and thermodynamics to be particularly lucid. Briefly, for the simple one-step binding scheme. 

Molecular recognition in biological systems (active sites on the surfaces of macromolecule, antibody-antigen) and biological sensors (enzyme activity, biosensors). 

Rini, J. M., U. Schulze-Gahmen, and I. A. Wilson, Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science 255 959-965, 1992. 

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