Biomolecular Interaction Analysis Core

Surface Plasmon Resonance (SPR) is used to monitor macromolecular interactions in real time. The Biacore systems use SPR technology for measuring the interactions of macromolecules with each other, and with small molecules. One of the molecular (ligand)is immobilized on carboxymethylated dextran over a gold surface while the second partner (analyte) flows over the immobilized ligand surface. The immobilized ligands are remarkably resilient and maintain their biological activity.

Interaction is detected via SPR, in real time, at high sensitivity, without the use of radioactivity. The bound analyte can be stripped from the immobilized ligand without affecting its activity to allow many cycles of binding and regeneration on the same immobilized surface. These instruments excel over most other methods of affinity measurements in that they are able to measure on-rates (ka in the range of 103 - 5x107M-1s-1) and off-rates (kd of 10-5 - 1 s-1).

Concentration determination experiments are also feasible. Some applications are:

  • Characterization of protein-protein interactions
  • Screen and selection of the best monoclonal antibodies
  • Identification of potential drug targets and diagnostic markers
  • Characterization of protein: small molecule interactions in drug discovery and selection of therapeutic candidates according to their on/off rates
Photo: Biacore T200 unit.

Biacore™ T200

Unit Description

Biacore T200 is a versatile, label-free system for detailed studies of biomolecular interactions. It has exceptional sensitivity, which enables interaction analysis with greater precision and confidence. It can be used to:

  • Obtain high quality kinetics from the fastest on-rates to the slowest off-rate
  • Analyze interactions involving the smallest low molecular weight compounds
  • Can process up to 384 samples in unattended runs
  • Has flexible software with high-level user guidance for fast assay development, analysis and evaluation
  • Has guided workflows with built-in data quality assessments and tools

Manufacturer Specifications

Please visit the GE Healthcare website for further information.


Rental available in one-day increments.


Please contact us to inquire about the rental of this equipment.

Isothermal Calorimetry

Isothermal titration calorimetry (ITC) instruments allow direct and label free measurement of binding affinity and thermodynamics. Heat released or absorbed during biochemical binding events is measured directly, giving information about relative binding affinity (KD), stoichiometry (N), enthalpy (ΔH), and entropy (ΔS). This information provides valuable insights into the mechanism of binding, including hydrogen bonding, van der Waals interactions, and hydrophobic interactions.

Some applications are:

  • Small molecule drug discovery
  • Validation of small molecule hits
  • Characterization of protein-protein interactions
  • Characterization of protein-nucleic acid interactions
  • Microcalorimetry of lipid membranes
  • Enzyme kinetics
  • Interaction between small molecules
  • Active concentration measurement


Photo: iTC200.

Unit description

  • Manufactured with Hastelloy cells that are chemically inert to biological materials
  • Cell loading volume of 300µL
  • Syringe loading volume 70µL
  • Automatic syringe loading and cleaning
  • active heating and cooling features leading to fast equilibration and experiment times; typical experiment takes 45 min
  • The software is user friendly and flexible i.e. experimental parameters (injection volume, duration, filter period, spacing etc) can be updated during a run
  • Origin 7.0 software offers advanced and customizable data analysis models including enzyme kinetics and sequential binding

Manufacturer Specifications

Please visit Malvern website for further information.


Rental available in one hour increments.


Please contact us to inquire about the rental of this equipment.