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Receptor clustering and dimerization

Understand receptor clustering and dimerization

A ligand-target interaction often changes in affinity and kinetics when the receptor shifts from a monomeric to a dimeric state, or when it forms clusters. This can be exploited to better understand your biological system. Investigate how drugs induce or prohibit dimerization or clustering by following the ligand binding, or label some ligands with quenchers* and study changes in proximity over time.

*only in LigandTracer Green

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By fitting the curve (green) to a model (black) it is possible to decipher the binding of EGF to EGFR monomers (blue), EGFR homodimers (orange) and EGFR-HER2 heterodimers (purple). The dimer ratios affect the overall binding and depend on hosting cell lines and their receptor population.

Gained information

  • Proximity of ligands caused by target clustering and dimerization
  • Effects of drugs inducing or preventing target clustering and dimerization
  • The impact of receptor populations on target clustering and dimerization
  • Avidity effects

Resources

Publications

A novel real-time proximity assay for characterizing multiple receptor interactions on living cells.
Bondza S, Björkelund H, Nestor M, Andersson K, Buijs J.
Anal Chem. 2017. 89(24):13212-13218
PubMed

Gefitinib induces epidermal growth factor receptor dimers which alters the interaction characteristics with 125I-EGF.
Björkelund H, Gedda L, Barta P, Malmqvist M, Andersson K.
PLoS ONE. 2011. 6(9): e24739.
PubMed