Literature about bivalent interaction and concentration

Hello,

I have seen the different kinetic models. In the bivalent model it is said.

In case of a bivalent interaction, the dependence of the concentration on the components of the interaction can be studied. At low analyte concentrations, the AB2 complex is dominating while at high analyte concentrations the AB complex is more abundant.

Someone have some literature about this.

Thank you everybody.

Papillon

Hi Papillon,

These references popped up:

1. Atwell, J. L. et al; Design and expression of a stable bispecific scFv dimer with affinity for both glycophorin and N9 neuraminidase. Mol.Immunol. (33): 1301-1312; 1996 - www.ncbi.nlm.nih.gov/cgi-bin/Entrez/refe...orm=6&uid=0009171890

2. Chen, G. et al; In vitro scanning saturation mutagenesis of all the specificity determining residues in an antibody binding site. Protein Eng (12): 349-356; 1999 - PM:0010325406

3. Iliades, P., Kortt, A. A., and Hudson, P. J.; Triabodies: single chain Fv fragments without a linker form trivalent trimers. FEBS Lett. (409): 437-441; 1997 - www.ncbi.nlm.nih.gov/cgi-bin/Entrez/refe...orm=6&uid=0009224705

4. Ito, W. and Kurosawa, Y.; Development of an artificial antibody system with multiple valency using an Fv fragment fused to a fragment of protein A. J.Biol.Chem. (268): 20668-20675; 1993 - www.ncbi.nlm.nih.gov/cgi-bin/Entrez/refe...orm=6&uid=0008376416

5. Noel, D. et al; Analysis of the individual contributions of immunoglobulin heavy and light chains to the binding of antigen using cell transfection and plasmon resonance analysis. J.Immunol.Methods (193): 177-187; 1996 - www.ncbi.nlm.nih.gov/cgi-bin/Entrez/refe...orm=6&uid=0008699031

6. Nygren, H., Werthen, M., and Stenberg, M.; Kinetics of antibody binding to solid-phase-immobilised antigen. Effect of diffusion rate limitation and steric interaction. J.Immunol.Methods (101): 63-71; 1987 -

7. Vauquelin, Georges and Charlton, Steven J.; Exploring avidity: understanding the potential gains in functional affinity and target residence time of bivalent and heterobivalent ligands. Br J Pharmacol n/a-n/a; 2013 - dx.doi.org/10.1111/bph.12106

Arnoud

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Jul 29 13 12:43 AM

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Hi Arnoud,

Thanks. I´ll see them.

Here are the right links:

1. Atwell, J. L. et al; Design and expression of a stable bispecific scFv dimer with affinity for both glycophorin and N9 neuraminidase. Mol.Immunol. (33): 1301-1312; 1996
www.ncbi.nlm.nih.gov/pubmed/9171890
www.sciencedirect.com/science/article/pii/S0161589096000971

2. Chen, G. et al; In vitro scanning saturation mutagenesis of all the specificity determining residues in an antibody binding site. Protein Eng (12): 349-356; 1999 - PM:0010325406
www.ncbi.nlm.nih.gov/pubmed/10325406

3. Iliades, P., Kortt, A. A., and Hudson, P. J.; Triabodies: single chain Fv fragments without a linker form trivalent trimers. FEBS Lett. (409): 437-441; 1997 - www.ncbi.nlm.nih.gov/pubmed/9224705

4. Ito, W. and Kurosawa, Y.; Development of an artificial antibody system with multiple valency using an Fv fragment fused to a fragment of protein A. J.Biol.Chem. (268): 20668-20675; 1993 -
www.ncbi.nlm.nih.gov/pubmed/8376416

5. Noel, D. et al; Analysis of the individual contributions of immunoglobulin heavy and light chains to the binding of antigen using cell transfection and plasmon resonance analysis. J.Immunol.Methods (193): 177-187; 1996
www.ncbi.nlm.nih.gov/pubmed/8699031

6. Nygren, H., Werthen, M., and Stenberg, M.; Kinetics of antibody binding to solid-phase-immobilised antigen. Effect of diffusion rate limitation and steric interaction.J.Immunol.Methods (101): 63-71; 1987 –
www.ncbi.nlm.nih.gov/pubmed/3611793
www.sciencedirect.com/science/article/pii/0022175987902171

Papillon

Thanks for the links.

Arnoud