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SKU: 3-04-002.
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Interaction Map

5002 000

Understand binding mechanisms and cell surface complexity with Interaction Map

Cell biology is intricate and sometimes there are not enough models to describe its complexity. Interaction Map is a plugin tool to TraceDrawer that analyze real-time binding curves without any a priori guesses of the binding mode. It displays a heat map in which peaks correspond to individual 1:1 binding events, for example ligands that not only interacts with receptor monomers but also with dimers, activated receptor forms, or completely different cell-surface associated proteins.  The kinetics, the affinity and prevalence of each binding mode is presented, together with its corresponding binding curve.

All in all, you get an image of function that helps you understand the binding mechanism and make better decisions in drug development and cell biology research. Its visual presentation of the data is perfect for communicating and convincing others.

Note that Interaction Map requires access to TraceDrawer.


Key features

  • Comprehensive visualization of the complexity in interactions and triggered effects
  • Suitable for investigation of avidity behavior
  • Compatible with many real-time data formats

Understanding the impact of dimerization on EGF binding

The interaction between EGF and EGFR is about 100 times more stable with EGFR-EGFR homodimers (left peak) than with EGFR monomers (right peak), resulting in a 100 times difference in affinity. Both interactions can occur simultaneously on A431 cells. The tyrosine kinase inhibitor erlotinib was found to induce dimers, observed as a shift towards the high affinity state, while lapatinib prevented dimer formation, shifting the interaction towards low affinity.




Publications describing Interaction Map. Please visit our list of publications to find more examples.

Deciphering complex protein interaction kinetics using Interaction Map.
Altschuh D, Björkelund H, Strandgård J, Choulier L, Malmqvist M, Andersson K.
Biochem Biophys Res Commun. 2012. 428(1):74-9.

Multivalent Fc-gamma-receptor engagement by a hexameric Fc-fusion protein triggers Fc-gamma-receptor internalisation and modulation of Fc-gamma-receptor functions.
Qureshi OS, Rowley TF, Junker F, Peters SJ, Crilly S, Compson J, Eddleston A, Björkelund H, Greenslade K, Parkinson M, Davies NL, Griffin R, Pither TL, Cain K, Christodoulou L, Staelens L, Ward E, Tibbitts J, Kiessling A, Smith B, Brennan FR, Malmqvist M, Fallah-Arani F, Humphreys DP.
Sci Rep. 2017. 7(1):17049.