Research and discovery

To be confident in your results you need robust and repeatable data. This is where Malvern Panalytical can help you in a number of ways, starting with understanding the quality and stability of assay components such as reagents, proteins or compounds. Reagent control is the basis for good assay development, and reagent stability, purity and functionality must be considered to achieve a robust assay. 

Watch the short videos, in the related content below, to see how our solutions can help with the following:

Make sure your target protein is in good condition  
When screening many compounds; for example, in a biosensor assay, it is critically important that the target protein is active and stable under assay conditions.  An unstable or inactive target protein could compromise the assay, resulting in costly screening iterations and potentially even false negative results. Learn how the Creoptix WAVE biosensor can aid your research.

Address solubility issues with low molecular weight ligands
Solubility issues for low molecular weight (LMW) ligands can also create quality issues in screening activities. Problems with solubility can affect binding data and make your ligand-ranking less reliable.   

Ensure all batches of target proteins are the same
Find out how Grating-Coupled Interferometry (GCI) and  Isothermal Titration Calorimetry  are used for quality control of different target protein batches.   

Enzymes play a special role in the human body by catalyzing chemical reactions through binding to molecular substrates and modifying them in specific ways. Enzymes are important in drug discovery and development, as approximately half of current drug targets are enzymes. A lot of effort is put into discovery and characterization of enzymatic pathways and enzyme activity as well as developing drugs that interact with enzymes 

Enzymatic assays are among the most frequently performed activities in biochemistry and typically require the use of labeled substrates and coupled reactions with spectrophotometric or chemical readout.  Isothermal titration calorimetry (ITC) offers a direct and generic way of following the rate of enzymatic catalysis through the heat rate associated with enzymatic reactions. Enzymatic assays in ITC can be run with opaque solutions at enzyme concentrations comparable to that used in biochemical assays and can yield a complete set of kinetic parameters in a single experiment.

Label-free, real-time binding kinetics

New within the Malvern Panalytical product range is the WAVEsystem. Based on Grating-Coupled Interferometry (GCI) technology, the WAVEsystem measures binding affinity and kinetics with unrivaled sensitivity. GCI technology combined with our microfluidic, no-clog cartridges makes the WAVEsystem a versatile platform that facilitates a broad range of research and discovery applications.

Mechanism of action (MOA) analysis helps develop the understanding of structure-activity relationships (SARs) for the target and any ligands. Isothermal Titration Calorimetry (ITC) is the gold standard technique for confirmation of the ligand’s direct binding to the target, measurement of co-factor binding, and differentiation between competitive, non-competitive and uncompetitive binding, as well as determination of the interaction stoichiometries. ITC provides a rapid thermodynamic characterization of the binding event.  

Now within the Malvern Panalytical product range is the WAVEsystem. Based on Grating-Coupled Interferometry (GCI) technology, the WAVEsystem measures binding affinity and kinetics with unrivaled sensitivity.

After fragment-based screening, the next step is understanding how to build on the fragment with different chemical functions to optimize the binding affinity of the compound. For this type of research, some analysts are using Isothermal Titration Calorimetry (ITC) to complement and guide SAR studies. This enables investigation of the entropy and enthalpy of the interaction between the compound and the target protein, which can inform us about changes in hydrogen bonds and hydrophobic interactions in the binding pocket, depending on which functional groups are added to the fragment.