Biomolecular interactions


MicroCal PEAQ-ITC (Malvern Panalytical)

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Biomolecular interactions

Kinetics and affinity

AlfatestLab uses 2 extremely versatile analytical techniques, ITC microcalorimetry and BioLayer Interferometry (BLI), to study interactions without molecular weight limits, in native conditions, label-free and in real time, in the mM-nM field. The techniques are compatible with a wide range of matrices, including organic solvents and non-purified samples, such as cell lysates, to offer a wide application versatility. It is also possible to analyse enzymatic kinetics, interactions with nanomaterials and other interaction phenomena between components in solution (micellization processes, dissociation, etc.). We offer the possibility to investigate a wide range of molecular interactions providing the direct measurement of affinity constants (KD) as well as the determination of the kinetic and/or thermodynamic profiles.

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BLI BioLayer Interferometry

Our Octet Red96 instrument, based on the BioLayer Interferometry technique, allows both the affinity and kinetics analysis. The technique uses specific sensors to immobilize one of the two interaction molecules. The sensors are available in a wide range of surface chemistries allowing to design complex and multistep experiments. The system enables the simultaneous analysis of 8 sensors using standard 96-well plates. This configuration is suitable for epitope binning or other screening experiments. The BLI technique is ideal to study complex samples and matrices as the signal is not influenced by the optical properties of the sample.

ITC Isothermal Titration Calorimetry

Isothermal Titration Calorimetry (ITC) is a technique used in quantitative studies of a wide variety of biomolecular interactions. It works by directly measuring the heat that is either released or absorbed during a biomolecular binding event.

ITC is the only technique that can simultaneously determine all binding parameters in a single experiment: affinity constant (KD), reaction stoichiometry (n), and thermodynamic parameters such as enthalpy (∆H) and entropy (ΔS) to elucidate the mechanisms underlying molecular interactions. Requiring no modification of binding partners, either with fluorescent tags or through immobilization, ITC measures the affinity of binding partners in their native states.