PEAQ-DSC

The high-sensitivity MicroCal PEAQ-DSC system features automated data analysis to support the generation of high-integrity thermal stability data and deliver compliance with regulatory requirements, whilst allowing easy integration into existing data handling and transfer systems.

Unattended operation of the instrument after sample loading frees operator time. This complete system requires no additional accessories, reagents or consumables.

The PEAQ-DSC Automated, with an autosampler, is also available.

Data generated by the MicroCal PEAQ-DSC provides critical guidance for biopharmaceutical development in protein engineering, (pre)formulation development, process development, manufacturing change control and biosimilarity and biocomparability studies. 

The integrated software streamlines workflows, facilitates non-subjective data analysis, performance qualification and compliance with 21 CFR Part 11 and Annex 11 regulations, all delivering high integrity data and driving productivity in biopharmaceutical research.

Powerful MicroCal PEAQ-DSC software minimizes typical data analysis time and includes:

• PEAQ-Compliance: The system is available with Malvern Access Controller (MAC) to limit access to user-defined SOPs and data analysis features. Data can be displayed using the Report Generator with user details and the ability to sign using electronic signatures to facilitate the integration of the workflow into your company’s quality system and aid compliance with 21 CFR Part 11 and Annex 11 regulations. This is provided as an optional accessory
• PEAQ-Performance: Automatically detects and validates system readiness for optimal performance
• PEAQ-Smart (including PEAQ-Finder): For SOP-based operation and data analysis.  Provides new algorithms to detect even subtle peaks and shoulders, facilitating the automatic, non-subjective identification of multiple transitions, such as those seen in multi-domain proteins
• PEAQ-Compare: For the quantitative comparison of DSC traces for comparability studies, ideal for batch-to-batch and biosimilarity studies
• Network-ready: email updates sent during the analysis to keep you informed of assay progress

Functional structures formed by proteins and other macromolecules often undergo temperature-induced conformational changes, such as unfolding. These changes result in the absorption of heat as a result of the redistribution of non-covalent bonds within the molecule. Differential Scanning Calorimeters measure this heat uptake very precisely.

The thermal core of the PEAQ-DSC system contains a sample cell (containing the sample of interest) and a reference cell (containing a matched buffer solution), both of which are housed within an insulating jacket. These two cells are always maintained at the same temperature, and during a measurement, they are heated at a constant scan rate. 

As the molecule within the sample cell unfolds, heat is absorbed, creating a temperature difference (ΔT) between the sample cell and the reference cell. This results in a thermal gradient across the Peltier units, creating a proportional voltage, which is in turn converted to power to form a feedback loop to the Peltier units, in order to return ΔT to zero.

Since protein unfolding is an endothermic event, it is observed as a positive displacement in the thermogram. The midpoint of this protein ‘melting’ transition is the T_m, and the area under the curve is the enthalpy (ΔH) of the unfolding process.