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An indirect method to measure trimerization constants using surface plasmon resonance
M Mattu1, C Bendtsen, G Barbato
1Biotechnology, IRBM, 00040 Pomezia, Italy.
The ability of surface plasmon resonance to precisely measure kinetic binding constants was exploited here to indirectly evaluate the thermodynamic dissociation trimerization constant (K(d)) of a designed chimeric protein, IZN-23, derived from an isoleucine zipper and a portion of the N-terminal helix residues of HIV-1 gp41. The method uses two monoclonal antibodies (mAbs) that display different off-rates when binding the monomeric or trimeric IZN-23. A detailed description of the data analysis strategy employed to unravel the K(d) trimerization constant from the observed off-rate kinetic values is presented, and the potential exploitation of this technique in different fields is highlighted.
The ability of surface plasmon resonance to precisely measure kinetic binding constants was exploited here to indirectly evaluate the thermodynamic dissociation trimerization constant (K(d)) of a designed chimeric protein, IZN-23, derived from an isoleucine zipper and a portion of the N-terminal helix residues of HIV-1 gp41. The method uses two monoclonal antibodies (mAbs) that display different off-rates when binding the monomeric or trimeric IZN-23. A detailed description of the data analysis strategy employed to unravel the K(d) trimerization constant from the observed off-rate kinetic values is presented, and the potential exploitation of this technique in different fields is highlighted.
