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Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR
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Insulin receptor-insulin interaction kinetics using multiplex surface plasmon resonance.

Kannan Subramanian1, Conan J Fee, Rayleen Fredericks

  • 1Biomolecular Interaction Centre and Department of Chemical and Process Engineering, University of Canterbury, Private Bag 4800, Christchurch, New Zealand, 8041.

Journal of Molecular Recognition : JMR
|November 27, 2013
PubMed
Summary

A new surface plasmon resonance (SPR) assay enables real-time study of insulin receptor interactions. This method advances understanding of type 2 diabetes by measuring insulin-eIR-A binding kinetics without labeling.

Keywords:
Lisproinsulininsulin receptorinteractionskineticssurface plasmon resonance

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Endocrinology

Background:

  • Type 2 diabetes impacts millions globally, necessitating deeper understanding of insulin receptor signaling.
  • Accurate measurement of insulin-insulin receptor kinetics is crucial for disease research.

Purpose of the Study:

  • To develop and validate a novel, rapid, real-time, multiplex surface plasmon resonance (SPR) assay.
  • To study the interaction kinetics between insulin and the insulin receptor ectodomain, isoform A (eIR-A).

Main Methods:

  • Utilized a scaffold approach with anti-insulin receptor antibody immobilization on an SPR sensorchip.
  • Employed a multiplex SPR system for parallel measurement of interactions.
  • Captured eIR-A and analyzed binding kinetics with recombinant human insulin and insulin analogue Lispro.

Main Results:

  • Recombinant human insulin exhibited a two-site binding pattern with high (K(D1) = 38.1 ± 0.9 nM) and low (K(D2) = 166.3 ± 7.3 nM) affinity sites.
  • Insulin analogue Lispro showed similar affinities (K(D1) = 73.2 ± 1.8 nM, K(D2) = 148.9 ± 6.1 nM).
  • Kinetic data for Lispro improved with a model incorporating a conformational change.

Conclusions:

  • The developed SPR assay provides a robust platform for real-time analysis of insulin-eIR-A interactions.
  • This assay can be extended to investigate the influence of humoral factors on insulin receptor binding.
  • The findings contribute to a better understanding of insulin dynamics in type 2 diabetes research.