Using Surface Plasmon Resonance to Quantitatively Assess Lipid-Protein Interactions

Kathryn Del Vecchio¹, Robert V Stahelin^{2

3}

Affiliations

¹ Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.
² Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA. rstaheli@iu.edu.
³ Department of Biochemistry and Molecular Biology, Indiana University School of Medicine-South Bend, 143 Raclin-Carmichael Hall, 1234 Notre Dame Avenue, South Bend, IN, 46617, USA. rstaheli@iu.edu.

PMID: 26552681
PMCID: PMC5964981
DOI: 10.1007/978-1-4939-3170-5_12

Using Surface Plasmon Resonance to Quantitatively Assess Lipid-Protein Interactions

Kathryn Del Vecchio et al. Methods Mol Biol. 2016.

. 2016:1376:141-53.

doi: 10.1007/978-1-4939-3170-5_12.

Authors

Kathryn Del Vecchio¹, Robert V Stahelin^{2

3}

Affiliations

¹ Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.
² Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA. rstaheli@iu.edu.
³ Department of Biochemistry and Molecular Biology, Indiana University School of Medicine-South Bend, 143 Raclin-Carmichael Hall, 1234 Notre Dame Avenue, South Bend, IN, 46617, USA. rstaheli@iu.edu.

PMID: 26552681
PMCID: PMC5964981
DOI: 10.1007/978-1-4939-3170-5_12

Abstract

Surface Plasmon Resonance (SPR) is a quantitative, label-free method for determining molecular interactions in real time. The technology involves fixing a ligand onto a senor chip, measuring a baseline resonance angle, and flowing an analyte in bulk solution over the fixed ligand to measure the subsequent change in resonance angle. The mass of analyte bound to fixed ligand is directly proportional to the resonance angle change and the system is sensitive enough to detect as little as picomolar amounts of analyte in the bulk solution. SPR can be used to determine both the specificity of molecular interactions and the kinetics and affinity of an interaction. This technique has been especially useful in measuring the affinities of lipid-binding proteins to intact liposomes of varying lipid compositions.

Keywords: Binding affinity; Equilibrium bind ing; Kinetics; Lipid–protein interactions; Surface plasmon resonance.

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Using Surface Plasmon Resonance to Quantitatively Assess Lipid-Protein Interactions

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Using Surface Plasmon Resonance to Quantitatively Assess Lipid-Protein Interactions

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