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Literature DB >> 9265731

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

Abstract

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.

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Year: 1997 PMID： 9265731 DOI： 10.1016/s0958-1669(97)80074-2

Source DB: PubMed Journal: Curr Opin Biotechnol ISSN： 0958-1669 Impact factor: 9.740

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Cited

40 in total

1. Combined affinity and rate constant distributions of ligand populations from experimental surface binding kinetics and equilibria.

Authors: Juraj Svitel; Andrea Balbo; Roy A Mariuzza; Noreen R Gonzales; Peter Schuck
Journal: Biophys J Date: 2003-06 Impact factor: 4.033

2. Refining the measurement of rate constants in the BIAcore.

Authors: David A Edwards
Journal: J Math Biol Date: 2004-04-23 Impact factor: 2.259

3. Simultaneous measurement of 10,000 protein-ligand affinity constants using microarray-based kinetic constant assays.

Authors: James P Landry; Yiyan Fei; Xiangdong Zhu
Journal: Assay Drug Dev Technol Date: 2011-12-22 Impact factor: 1.738

Review 4. Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.

Authors: Bram Stynen; Hélène Tournu; Jan Tavernier; Patrick Van Dijck
Journal: Microbiol Mol Biol Rev Date: 2012-06 Impact factor: 11.056

Review 5. Opportunities and Challenges for Biosensors and Nanoscale Analytical Tools for Pandemics: COVID-19.

Authors: Nikhil Bhalla; Yuwei Pan; Zhugen Yang; Amir Farokh Payam
Journal: ACS Nano Date: 2020-06-26 Impact factor: 15.881

6. Probing the functional heterogeneity of surface binding sites by analysis of experimental binding traces and the effect of mass transport limitation.

Authors: Juraj Svitel; Hacène Boukari; Donald Van Ryk; Richard C Willson; Peter Schuck
Journal: Biophys J Date: 2006-12-08 Impact factor: 4.033

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

1. Combined affinity and rate constant distributions of ligand populations from experimental surface binding kinetics and equilibria.

2. Refining the measurement of rate constants in the BIAcore.

3. Simultaneous measurement of 10,000 protein-ligand affinity constants using microarray-based kinetic constant assays.

Review 4. Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.

Review 5. Opportunities and Challenges for Biosensors and Nanoscale Analytical Tools for Pandemics: COVID-19.

6. Probing the functional heterogeneity of surface binding sites by analysis of experimental binding traces and the effect of mass transport limitation.

7. Temperature effects on DNA chip experiments from surface plasmon resonance imaging: isotherms and melting curves.

8. PROBING αIIbβ3: LIGAND INTERACTIONS BY DYNAMIC FORCE SPECTROSCOPY AND SURFACE PLASMON RESONANCE.

Review 9. Suboptimal engagement of the T-cell receptor by a variety of peptide-MHC ligands triggers T-cell anergy.

10. Bayesian analysis of heterogeneity in the distribution of binding properties of immobilized surface sites.