Biomolecular Interactions Service Lab (Biacore)


  • Ferenc Erdődi (head of the laboratory)
  • Bálint Bécsi

In both basic and applied science it is often required to uncover the mechanism of protein-protein and protein-ligand interactions. Surface plasmon resonance based binding study is the choice of technique nowadays for these studies since this measurement requires  relatively low amount of samples and it can provide quantitative kinetic and thermodynamic data for the interaction of the binding partners.

In the Biomolecular Interaction Laboratory we study and characterize the interaction of biomolecules using Biacore-3000 equipment based on the principles of surface plasmon resonance. To carry out such studiesrelatively low amount of the binding partners are needed.One of the binding partners is immobilized on the surface of a sensor chip by covalent coupling, then the solution containing the other partner is injected over the surface and the interaction is detected and quantified. The equipment is suitable for multi-chanell analyses at wide temperature (4-40oC) and flow rate (1-2 ml/min to 50-100 ml/min) range. It is also able to detect relatively weak (Ka~104) interactions. The equipment is supplied with a user friendly software which makes possible the evaluation of the binding data for different kinetic mechanisms.

Recently, MicroCal iTC200 equipment suitable for measuring heat changes during isothermal titration calorymetry (ITC) was also installed in the laboratory that complemented the services to offer. This technique requires relatively low amount of samples for the measurements and still can provide quantitative data for the interaction of the binding partners. This ITC-based MicroCal iTC200 is suitable for the simultaneous determination of binding parameters such as association constant (K), the stoichiometry (n, mol/mol binding), enthalpy (ΔH) and entropy change (ΔS) of the interaction. The equipment directly measures sub-millimolar to nanomolar binding constants (102 to 109 M-1) and also suitable to measure nanomolar to picomolar binding constants using competitive binding technique (109 to 1012 M-1). Experiments require only 200 μl of sample and as little as 5-10 μg of protein can be used in the sample cell. It is a true in-solution technique: no immobilization or labeling required, there are no buffer restrictions and even turbid solutions can also be handled easily. Most of the interactions listed as provided services below can be studied by both SPR- or ITC- based techniques. The two techniques complement each other too, since kinetic data are generally available from SPR measurements, while thermodynamic data are more reliably obtained by ITC technique. In addition ITC is suitable to determine interactions as weak as 102 M-1, while the limit is 104 M-1 in SPR experiments.

Services provided, conditions and charges

Access to measurments includes service charge and the conditions and time for the services are required to set in advance with the staff of the laboratory. The Biomolecular Interaction Laboratory provides the following services:

  • quantitative characterization of protein-protein and protein-ligand interactions using purified components: determination of the association and dissociation rate constants as well as the association/dissociation constants for the interaction
  • characterization of antigen-antibody interaction including epitope mapping
  • study of the binding of possible drug molecules to the target protein and /or to receptor
  • characterization of protein-nucleic acid and protein-carbohydrate interactions
  • separation protein(s) that bind to an immobilized partner from cell lysate or partially purified samples via a sample recovering system: binding proteins are recovered in a form suitable for analyses by mass spectrometry or by immunological methods.

The following charges are applied for the services

Work Unit Price (HUF)
Equipment usage time  hour 6 000
Immobilization 1 chip/4 surfaces 15 000
Data evaluation             1 concentration series   18 000
   (min. 3, max 7 conc.)
Evaulation time   hour 6 000
MicroCal ITC200
Equipment usage time hour 6 000
Data evaluation 1 ligand titration 3000 with 1 interacting partner


Frissítés dátuma: 2017.07.19.