MicroCal PEAQ-ITC Automated

In this application note, discover how to perform enzyme kinetics experiments with a MicroCal isothermal titration calorimetry (ITC) system.

Isothermal titration microcalorimetry (ITC) is an essential tool in drug discovery and the study and regulation of protein interactions. This brochure describes how Malvern MicroCal ITC calorimeters are designed to deliver the exceptional performance and outstanding quality data needed in these application areas.

In this application note, Malvern Panalytical discuss how isothermal titration calorimetry (ITC) can be used to determine the contribution of individual protein residues or modifications to the total binding affinities of complex substrates. Incorporating binding, thermodynamic and stoichiometry data from ITC, structural studies like NMR and X-ray crystallography, and in vivo studies, will ultimately lead to a complete understanding of these complex interactions.

In this application note, practical tips are provided for scientists conducting Isothermal titration calorimetry. These tips pertain to things such as:

• The removal of bubbles
• Residual solution in the ITC cell
• Remaining sample solution in a cell reservoir
• Importance of cleaning the cell reservoir and pipette retaining nut
• Washing and rinsing error troubleshooting

Unfolded proteins fold into thermodynamically-favorable native structures under the correct physiological conditions for gain of function. This whitepaper describes how differential scanning calorimetry and isothermal titration calorimetry can be used as a powerful method for the thermodynamic investigation of interactions between diverse biomolecules and inorganic compounds. It details some examples from literature of the methods application in studying amyloid fibrillation.

This whitepaper outlines how two different approaches can be combined to provide a data-analysis strategy of superior reproducibility and without user bias, as the only user input required is the calorimetric dataset itself. Many industrial and biochemical applications depend on the usage of detergents and other surfactants. These compounds are indispensable, in particular, for the extraction, purification, and handling of membrane proteins. Owing to their amphiphilic nature, detergents can provide a membrane-mimetic environment required by integral membrane proteins to retain their native structures and functions in aqueous solution. The CMC is one of the most fundamental characteristics of a surfactant. In aqueous solutions, surfactants form colloidal aggregates, so-called micelles, when their concentration exceeds the CMC. To obtain the CMC in an accurate and precise manner, however, isothermal titration calorimetry (ITC) is the method of choice, which is due to its extraordinary sensitivity, unsurpassed resolution, and high reproducibility.

Isothermal titration calorimetry (ITC) is an analytical technique that has become the “gold standard” for studying intermolecular interactions. As its name indicates, it is a titrimetric technique, that is, a volumetric laboratory method for quantitative chemical analysis (traditionally intended to determine the unknown concentration of an identified analyte) where a reagent solution, the titrant, is made to react with a solution of analyte or titrand. This white paper details the use of ITC in biophysical studies.

Measurements and characterization of binding interactions between proteins and low-molecular weight ligands are fundamental for drug discovery. Among the most recognized challenges in characterizing binding interactions are (1) the need to accurately assess a wide span of binding affinities (KD) and (2) accurately rank and characterize low-molecular weight (LMW) ligands based on affinity, mechanism of action, and energetics of interaction.

Measurement and characterization of binding interactions between proteins and low-molecular weight (LMW) ligands are a focus of academic research and drug discovery. Isothermal titration calorimetry (ITC) directly measures heat released or absorbed in a binding event, providing means for studying protein-small molecule interactions in solution without the need for labeling or immobilization. Importantly, ITC is often utilized to characterize differences in entropic and enthalpic contributions to binding of novel ligands.

This Malvern Panalytical masterclass delves into the intricacies of interaction analysis and explores how ITC and GCI are complementary and orthogonal techniques for all early-stage drug discovery needs. Discover how ITC and GCI technologies can be applied to complex targets and interactions in a series of applications from hit identification to lead-optimization.

Over the last twenty years, Fragment-based drug design (FBDD) has emerged as a prominent strategy. Yet FBDD is not without challenges, including commercial libraries often hampered by excessively sized fragments. Recently new assaying techniques have emerged that push the boundaries of what’s possible with fragment screening, offering collections specifically tailored to biophysical screening. In this webinar, two respected industry authorities reveal how next-generation FBDD fragment screening can assist biophysical researchers more efficiently identify and prioritize the best fragment hits, compress hit-to-lead campaign times, and reduce research cost and raise lead throughput.

Learn more about the MicroCal PEAQ-ITC, the most advanced Isothermal Titration Calorimetry system from Malvern Instruments, which offers high quality data, ease of use, and exceptional sensitivity. Suited to life sciences and drug discovery applications, this microcalorimetry instrument is perfect for researchers wishing to study biomolecular interactions.

Resolving challenges, finding solutions