Antibody recognition

Mariuzza, R.A., Phillips, S.E.V., Poljak, R.J. The structural basis of antigen-antibody recognition. Annu. Rev. Biophys. Biophys. Chem. 16 139-159, 1987. 

Carr DJJ, DeCosta BR, Kim C-H, Jacobson AE, Bost KL, Rice KC, Blalock JE (1990) Antiopioid receptor antibody recognition of a binding site on brain and leukocyte opioid receptors. Neuroendocrinology 51 552-560... 

Lutz, K.L. Szabo,L. A. Thompson, D.L. Siahaan, T. J., Antibody recognition of peptide sequence from the cell-cell adhesion proteins N- and E-cadherins, Peptide Res. 9, 233-239 (1996). 

Badley, J.E., Grieve, R.B., Bowman, D.D., Glickman, L.T. and Rockey,J.H. (1987) Analysis of Toxocara canis larval excretory-secretory antigens physicochemical characterization and antibody recognition. Journal of Parasitology 73, 593-600. 

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... 

Varma, M. M. Nolte, D. D. Inerowicz, H. D. Regnier, F. E., Spinning disk self referencing interferometry of antigen antibody recognition, Opt. Lett. 2004, 29, 950 952... 

Antibody interaction drug delivery, 9 64 Antibody purification, 14 145 Antibody recognition, recombinant phage screening by, 12 506-507 Anticakes, for sodium nitrite, 22 857 Anticaking agents, 12 31, 63... 

Antigen antibody recognition is dependent on protein structure. A conformational change in a protein caused by formalin fixation may mask the epitope and thus affect the antigenicity of proteins in formalin-treated tissue (Montero 2003). The antigen retrieval leads to a renaturation or at least partial restoration of the protein structure, with re-establishment of the three-dimensional protein structure to something approaching its native condition (Shi et al. 1991). 

Fig. 4 Lerner s group used phosphonate [3] as the hapten to raise an antibody which was capable of hydrolysing the ester [5] shown alongside it. Schultz found that naturally occurring antibodies using phosphate [4] as their antigen could hydrolyse the corresponding p-nitrophenyl choline carbonate [6]. (Those parts of haptens [3] and [4] required for antibody recognition have been emphasized with bold bonds.)...

For all these reasons, some chemical or genetical modifications have been applied into the binding sites of antibodies in order to improve their reactivity [22]. Antibodies can be modified by the incorporation of natural or synthetic catalysts into the antibody recognition site, as for instance transition metal complexes, cofactors, and bases or nucleophiles, to carry other catalytic functions, which open the way to... 

From the results reported to date, it seems that the manner in which haptens are attached to carrier proteins leads to significant differences in certain cases. Clearly, haptens designed with aromatic moieties between the linkage to the immunogenic carrier protein and the TSA motif often have better antibody recognition. Recently, Hilvert pointed out that on both micro and macro levels, mechanistic improvements arise as a function of time. The differences in time scales for the evolution of natural enzymes and antibodies — millions of years versus weeks or months — also appear to be an explanation of the low efficiency of antibody catalysts. He also highlighted that the unique immunoglobulin fold has not been adopted by nature as one of the common scaffolds on which to build enzyme catalytic machinery. Therefore, antibody structure itself places limitations on the kind of reactions amenable to catalysis. 

In addition, the polymer-coated adenovirus particles were able to shield against antibody recognition. In another approach, the PEGylation of the adenovirus capsid protein prolonged transgene expression after systemic delivery of El-deleted adenovirus, and allowed partial readministration with native virus (50). Adenovirus has been explored as vector for the treatment of cystic fibrosis (51), for Duchenne muscular dystrophy (52), to deliver tumor suppressor genes for cancer treatment... 

Antibody recognition in organic media is poor due to partial or total denaturalization but MIPs perform very well in non-aqueous solvents broadening the application of MIP-ILAs only to analytes soluble in organic media. 

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