Reliable determination of binding affinity and kinetics using surface plasmon resonance biosensors.

Progress has been made in the identification of experimental and analytical procedures that allow for a more reliable determination of equilibrium and kinetic constants. Possible origins of the frequently observed deviations of the measured binding progress from that expected for chemical binding of pseudo-first order, and appropriate experimental controls have been proposed. Improved analytical approaches include the application of global analysis and analytical corrections for the influence of mass transport.

[1]  M L Yarmush,et al.  An analysis of transport resistances in the operation of BIAcore; implications for kinetic studies of biospecific interactions. , 1996, Molecular immunology.

[2]  G M Whitesides,et al.  A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance. , 1996, Analytical chemistry.

[3]  R. Fisher,et al.  Surface plasmon resonance based methods for measuring the kinetics and binding affinities of biomolecular interactions. , 1994, Current opinion in biotechnology.

[4]  R. Karlsson,et al.  Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. , 1997, Journal of immunological methods.

[5]  R W Glaser,et al.  Antigen-antibody binding and mass transport by convection and diffusion to a surface: a two-dimensional computer model of binding and dissociation kinetics. , 1993, Analytical biochemistry.

[6]  R J Leatherbarrow,et al.  Kinetics of protein-protein interactions at the surface of an optical biosensor. , 1995, Analytical biochemistry.

[7]  P. Garland,et al.  Optical evanescent wave methods for the study of biomolecular interactions , 1996, Quarterly Reviews of Biophysics.

[8]  R. Karlsson,et al.  Kinetic and Concentration Analysis Using BIA Technology , 1994 .

[9]  A. Plant,et al.  Phospholipid/alkanethiol bilayers for cell-surface receptor studies by surface plasmon resonance. , 1995, Analytical biochemistry.

[10]  G. Hausdorf,et al.  Binding kinetics of an antibody against HIV p24 core protein measured with real-time biomolecular interaction analysis suggest a slow conformational change in antigen p24. , 1996, Journal of immunological methods.

[11]  B. Persson,et al.  Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins , 1991 .

[12]  D. Margulies,et al.  Studying interactions involving the T-cell antigen receptor by surface plasmon resonance. , 1996, Current opinion in immunology.

[13]  P. Schuck,et al.  Kinetics of ligand binding to receptor immobilized in a polymer matrix, as detected with an evanescent wave biosensor. I. A computer simulation of the influence of mass transport. , 1996, Biophysical journal.

[14]  C. Maule,et al.  Detection and quantification of biomolecular interactions with optical biosensors , 1995 .

[15]  J. Casas-Finet,et al.  Real-Time BIAcore Measurements of Escherichia coli Single-Stranded DNA Binding (SSB) Protein to Polydeoxythymidylic Acid Reveal Single-State Kinetics with Steric Cooperativity , 1994 .

[16]  A. Kortt,et al.  Identification and minimization of nonideal binding effects in BIAcore analysis: ferritin/anti-ferritin Fab' interaction as a model system. , 1997, Analytical biochemistry.

[17]  C. DeLisi,et al.  The biophysics of ligand–receptor interactions , 1980, Quarterly Reviews of Biophysics.

[18]  D. Myszka,et al.  Kinetic analysis of ligand binding to interleukin‐2 receptor complexes created on an optical biosensor surface , 1996, Protein science : a publication of the Protein Society.

[19]  D. Winzor,et al.  Use of a resonant mirror biosensor to characterize the interaction of carboxypeptidase A with an elicited monoclonal antibody. , 1997, Analytical biochemistry.

[20]  Tony K. Quon,et al.  Software for Modeling Kinetic Phenomena , 1996 .

[21]  John Crank,et al.  The Mathematics Of Diffusion , 1956 .

[22]  J. Schlessinger,et al.  Measurement of the binding of tyrosyl phosphopeptides to SH2 domains: a reappraisal. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[23]  D. Winzor,et al.  Studies of protein interactions by biosensor technology: an alternative approach to the analysis of sensorgrams deviating from pseudo-first-order kinetic behavior. , 1997, Analytical biochemistry.

[24]  Z. Salamon,et al.  Surface plasmon resonance studies of complex formation between cytochrome c and bovine cytochrome c oxidase incorporated into a supported planar lipid bilayer. I. Binding of cytochrome c to cardiolipin/phosphatidylcholine membranes in the absence of oxidase. , 1996, Biophysical journal.

[25]  J. Cann,et al.  Demonstration of an upper limit to the range of association rate constants amenable to study by biosensor technology based on surface plasmon resonance. , 1996, Analytical biochemistry.

[26]  H. Vogel,et al.  Covalent attachment of functionalized lipid bilayers to planar waveguides for measuring protein binding to biomimetic membranes , 1995, Protein science : a publication of the Protein Society.

[27]  C. MacKenzie,et al.  Analysis by Surface Plasmon Resonance of the Influence of Valence on the Ligand Binding Affinity and Kinetics of an Anti-carbohydrate Antibody (*) , 1996, The Journal of Biological Chemistry.

[28]  P. Schuck,et al.  Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules. , 1997, Annual review of biophysics and biomolecular structure.

[29]  A. Archakov,et al.  Immobilization of proteins to lipid bilayers. , 1996, Biosensors & bioelectronics.

[30]  S. Gorti,et al.  Probe diffusion in an aqueous polyelectrolyte solution , 1985 .

[31]  M Brigham-Burke,et al.  Detection and quantitation of hexa-histidine-tagged recombinant proteins on western blots and by a surface plasmon resonance biosensor technique. , 1995, Analytical biochemistry.

[32]  L. Nieba,et al.  Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics. , 1996, Analytical biochemistry.

[33]  A. Barclay,et al.  Analysis of cell-adhesion molecule interactions using surface plasmon resonance. , 1996, Current opinion in immunology.

[34]  G. Gerisch,et al.  Oriented binding of a lipid-anchored cell adhesion protein onto a biosensor surface using hydrophobic immobilization and photoactive crosslinking. , 1996, Analytical biochemistry.

[35]  E. Goldman,et al.  A mutational analysis of the binding of two different proteins to the same antibody. , 1996, Biochemistry.

[36]  A. Minton,et al.  Analysis of mass transport-limited binding kinetics in evanescent wave biosensors. , 1996, Analytical biochemistry.

[37]  D. Winzor,et al.  Interpretation of deviations from pseudo-first-order kinetic behavior in the characterization of ligand binding by biosensor technology. , 1996, Analytical biochemistry.

[38]  D. O'Shannessy,et al.  Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: a critique of the surface plasmon resonance literature. , 1994, Current opinion in biotechnology.

[39]  P. Gershon,et al.  Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance detector. , 1995, Journal of immunological methods.

[40]  A. Malmborg,et al.  BIAcore as a tool in antibody engineering. , 1995, Journal of immunological methods.

[41]  R. Karlsson,et al.  Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. , 1991, Journal of immunological methods.