Using surface plasmon resonance to quantitatively assess lipid–protein interactions

Kathryn Del Vecchio, Robert V. Stahelin

Research output: Chapter in Book/Report/Conference proceedingChapter

10 Scopus citations


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.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Number of pages13
StatePublished - 2016

Publication series

NameMethods in Molecular Biology
ISSN (Print)10643745


  • Binding affinity
  • Equilibrium binding
  • Kinetics
  • Lipid–protein interactions
  • Surface plasmon resonance

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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  • Cite this

    Del Vecchio, K., & Stahelin, R. V. (2016). Using surface plasmon resonance to quantitatively assess lipid–protein interactions. In Methods in Molecular Biology (Vol. 1376, pp. 141-153). (Methods in Molecular Biology; Vol. 1376). Humana Press Inc..