Online optimization of surface plasmon resonance-based biosensor experiments for improved throughput and confidence.
The emergence of surface plasmon resonance-based optical biosensors has facilitated the identification of kinetic parameters for various macromolecular interactions. Normally, these parameters are determined from experiments with arbitrarily chosen periods of macromolecule and buffer injections, and varying macromolecule concentrations. Since the choice of these variables is arbitrary, such experiments may not provide the required confidence in identified kinetic parameters expressed in terms of standard errors. In this work, an iterative optimization approach is used to determine the above-mentioned variables so as to reduce the experimentation time, while treating the required standard errors as constraints. It is shown using multiple experimental and simulated data that the desired confidence can be reached with much shorter experiments than those generally performed by biosensor users.
De Crescenzo
Gregory
G
Department of Chemical Engineering, Ecole Polytechnique de Montréal, P. O. Box 6079, Centre-ville Station, Montréal, Québec, Canada H3C 3A7. gregory.decrescenzo@polymtl.ca
Woodward
Lyne
L
Srinivasan
Bala
B
D000818:Animals; D000911:Antibodies, Monoclonal; D000954:Antigens, Surface / Q000737:chemistry; D043425:Glutamate Carboxypeptidase II / Q000737:chemistry; D006801:Humans; D007700:Kinetics; D008297:Male; D051379:Mice; D008962:Models, Theoretical; D046912:Multiprotein Complexes; D009842:Oligopeptides / Q000737:chemistry; D009862:Online Systems; D020349:Surface Plasmon Resonance / Q000379:methods* / Q000706:statistics & numerical data; D013816:Thermodynamics
D000911:Antibodies, Monoclonal; D000954:Antigens, Surface; D046912:Multiprotein Complexes; D009842:Oligopeptides; C473848:FOLH1 protein, human; D043425:Glutamate Carboxypeptidase II