Mechanistic studies of electrostatic potentials on antigen--antibody complexes for bioanalyses.
A concept involving the use of antibodies conjugated with reporter molecules for the direct sensing on the subtle changes in the local electrostatic environment of antigen-antibody complexes due to the antigen binding was proposed and demonstrated. The studies including the effect of solution conditions on the extent and magnitude of the electrostatic potentials around the antigen-antibody complex and the quantitative dependence of the distance between the reporter molecule and the antigen-antibody binding site on the effectiveness of the reporter molecule for sensing the antigen-antibody binding event are presented and discussed. Basic understanding of induced changes in the electrostatic potentials on the antigen-antibody complex is essential for implementing the proposed direct sensing mechanism.
Huang
P Y
PY
Department of Chemical and Biochemical Engineering, University of Maryland, Baltimore 21228.
Lee
C S
CS
D000595:Amino Acid Sequence; D000936:Antigen-Antibody Complex; D001665:Binding Sites; D004563:Electrochemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007074:Immunoglobulin G; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D013205:Staphylococcal Protein A
D000936:Antigen-Antibody Complex; D007074:Immunoglobulin G; D010446:Peptide Fragments; D013205:Staphylococcal Protein A