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Label-free quantification of membrane-ligand interactions using backscattering interferometry

Academic Article
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Overview

authors

  • Baksh, M. M.
  • Kussrow, A. K.
  • Mileni, M.
  • Finn, M.G.
  • Bornhop, Darryl

publication date

  • April 2011

journal

  • Nature Biotechnology  Journal

abstract

  • Although membrane proteins are ubiquitous within all living organisms and represent the majority of drug targets, a general method for direct, label-free measurement of ligand binding to native membranes has not been reported. Here we show that backscattering interferometry (BSI) can accurately quantify ligand-receptor binding affinities in a variety of membrane environments. By detecting minute changes in the refractive index of a solution, BSI allows binding interactions of proteins with their ligands to be measured at picomolar concentrations. Equilibrium binding constants in the micromolar to picomolar range were obtained for small- and large-molecule interactions in both synthetic and cell-derived membranes without the use of labels or supporting substrates. The simple and low-cost hardware, high sensitivity and label-free nature of BSI should make it readily applicable to the study of many membrane-associated proteins of biochemical and pharmacological interest.

subject areas

  • Amidohydrolases
  • Cholera Toxin
  • G(M1) Ganglioside
  • Humans
  • Interferometry
  • Kinetics
  • Ligands
  • Membrane Proteins
  • Microscopy, Fluorescence
  • Protein Binding
  • Receptors, CXCR4
  • Receptors, GABA-B
  • Refractometry
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Identity

PubMed Central ID

  • PMC3246389

International Standard Serial Number (ISSN)

  • 1087-0156

Digital Object Identifier (DOI)

  • 10.1038/nbt.1790

PubMed ID

  • 21399645
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Additional Document Info

start page

  • 357

end page

  • 360

volume

  • 29

issue

  • 4

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