Srilatha, Nonavinakere Seetharam and Murthy, Gundlupet Satyanarayana (2006) Electrostatic Interaction in BIAcore Binding Studies: A Cause for Anomaly. In: Current Science, 90 (5). pp. 677-682.
Sensograms of human chorionic gonadotropin–monoclonal antibody (hCG–MAb); ligand–ligate binding in the BIAcore were analysed. Surface-bound MAb in 0.1 M phosphate buffer was unaltered by the concentration of MAb $(C_M_A_b)$ as well as pH of the sensogram. Surprisingly, at 0.01 M phosphate buffer concentration surface-bound MAb markedly decreased (300%) at pH 9. At low ionic strength Bovine Serum Albumin (BSA), a nonspecific protein, bound to the uncoupled (control channel) chip at pH 5, but not at 7. BSA so bound did show a dissociation profile like MAb, with fast and slow dissociating components. Binding of BSA to the chip at low ionic strength clearly stablished the presence of salt-dependent interaction between the protein and chip matrix. A model is proposed which rationally explains, on the basis of electrostatic interaction, the association and dissociation anomalies often encountered in the BIAcore sensograms.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this artcle belongs to Indian Academy of Sciences.|
|Keywords:||BIAcore; human chorionic gonadotropin; matrix-ligate interaction; monoclonal antibodies;Human chorionic-gonadotropin;Antigen-antibody interaction;Surface-plasmon resonance;Biosensor technology;Kinetic-analysis;Epitope;Complex;Subunit;Alpha|
|Department/Centre:||Division of Biological Sciences > Molecular Reproduction, Development & Genetics (formed by the merger of DBGL and CRBME)|
|Date Deposited:||23 Jan 2007|
|Last Modified:||19 Sep 2010 04:28|
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