Optical Biosensor Techniques to Analyze Protein-Polysaccharide Interactions

  • David G. Fernig
Part of the Methods in Molecular Biology™ book series (MIMB, volume 171)


Networks of interacting molecules, operating from the outside of the cell to the cell nucleus, regulate cell behavior. Optical biosensors provide a means of analyzing these interactions and possess key advantages over other methods: posttranslationally modified proteins, secondary gene products such as polysaccharides, chemically synthesized molecules, and nucleic acids are all equally susceptible to analysis; a quantitative description of an interaction is obtained; the structural rules and the kinetics governing the formation of multimolecular assemblies can be probed.


Bulk Phase Evanescent Wave Sensor Surface Optical Biosensor Immobilize Ligand 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


  1. 1.
    Schuck, P. (1997) Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules. Annu. Rev. Biophys. Biomol. Struct. 26, 541–566.PubMedCrossRefGoogle Scholar
  2. 2.
    Peters, T. (1996) All About Albumin: Biochemistry, Genetics, and Medical Applications. Academic Press, San Diego, CA.Google Scholar
  3. 3.
    Rahmoune, H. J., Gallagher, T., Rudland, P. S., and Fernig, D. G. (1998) Interaction of heparan sulphate from mammary cells with extracellular regulatory proteins. Acidic and fibroblast growth factor: regulation of the activity of bFGF by high and low affinity binding sites in heparan sulphate. J. Biol. Chem. 273, 7303–7310.PubMedCrossRefGoogle Scholar
  4. 4.
    Kinsella, L., Chen, H.-L., Smith, J. A., Rudland, P. S., and Fernig, D. G. (1998) Interactions of putative heparin-binding domains of basic fibroblast growth factor and its receptor, FGFR1, with heparin using synthetic peptides. Glycoconjugate J. 15, 419–422.CrossRefGoogle Scholar
  5. 5.
    Courty, J. M., Dauchel, C., Caruelle, D., Perderiset, M., and Barritault, D. (1991). Mitogenic properties of a new endothelial-cell growth-factor related to pleiotrophin. Biochem. Biophys. Res. Commun. 180, 145–151.PubMedCrossRefGoogle Scholar
  6. 6.
    Vacherot, F., Delbe, J., Heroult, M., Barritault, D., Fernig, D. G. and Courty, J. (1999) Glycosaminoglycans differentially bind HARP and modulate its biological activity. J. Biol. Chem. 274, 7741–7747.PubMedCrossRefGoogle Scholar
  7. 7.
    Edwards, P. R., Gill, A., Pollardknight, D. V., Hoare, M., Buckle, P. E., Lowe, P. A., and Leatherbarrow, R. J. (1995) Kinetics of protein-protein interactions at the surface of an optical biosensor. Anal. Biochem. 231, 210–217.PubMedCrossRefGoogle Scholar
  8. 8.
    Sadir, R., Forest, E., and LortatJacob, H. (1998) The heparan sulfate binding sequence of interferon-gamma increased the on rate of the interferon-gamma-interferon-gamma receptor complex formation. J. Biol. Chem. 273, 10919–10925.PubMedCrossRefGoogle Scholar

Copyright information

© Humana Press Inc., Totowa, NJ 2001

Authors and Affiliations

  • David G. Fernig
    • 1
  1. 1.School of Biological SciencesUniversity of LiverpoolLiverpoolUK

Personalised recommendations