AVS 56th International Symposium & Exhibition
    Biomaterial Interfaces Wednesday Sessions
       Session BI+AS+NS-WeA

Paper BI+AS+NS-WeA12
Label-Free Determination of Protein-Ligand Equilibrium in Aqueous Solution using Overlayer Enhanced Attenuated Total Reflectance Fourier Transform Infrared Spectroscopy (OE-ATR-FTIR)

Wednesday, November 11, 2009, 5:40 pm, Room K

Session: Quantitative Nanoscale Sensing at Biosurfaces and Interfaces
Presenter: T.C. Ruthenburg, University of California, Davis
Authors: T.C. Ruthenburg, University of California, Davis
S.S.N. Park, University of California, Davis
T.A. Aweda, University of California, Davis
C.F. Meares, University of California, Davis
D.P. Land, University of California, Davis
Correspondent: Click to Email
Protein binding/affinity studies are often performed using Surface Plasmon Resonance techniques that don't produce much spectral information. Measurement of protein binding affinity using FTIR is traditionally performed using high protein concentration or deuterated solvent. By immobilizing a protein near the surface of a gold-coated germanium internal reflection element interactions can be measured between an immobilized protein and small molecules in aqueous solution. Using flow injection analysis the on and off rates of these interactions and dissociation constant for the system can be determined. The dissociation constant for the molecule Yttrium-aminobenzyl-DOTA binding to the antibody 2D12.5 system was determined.