DSC (Differential Scanning Calorimetry) Analysis

DSC (Differential Scanning Calorimetry) can be used for the thermal stability analysis of biomolecules. Proteins transform from their native folded conformation to a denatured unfolded conformation (random coil, etc.) at a constant heating rate; DSC instruments monitor and record the changes in heat capacity of protein drugs with temperature in real time; thermodynamic information such as Tm value, Tonset, ΔH, and ΔCp can be obtained through data processing (e.g., integration). Various biophysical methods can be used to comprehensively characterize the higher-order structural stability of biomolecules. Among them, differential scanning calorimetry (DSC) is a recognized method for conformational stability analysis; Malvern Panaco's PEAQ-DSC automated system features an autosampler, eliminating the need for manual operation and simplifying the workload of screening large batches of samples. DSC provides a wealth of thermodynamic information, including Tm values, enthalpy change, and T1/2, enabling a comprehensive understanding of protein conformational stability. DSC technology is widely used in the field of protein drugs, including monoclonal antibodies, bispecific antibodies, ADCs, and vaccines. It also plays a crucial role in the characterization of nucleic acid delivery vectors. Due to the complexity of biomolecules, we should also employ complementary techniques based on multiple complementary principles to conduct a more comprehensive assessment of higher-order structural stability.

Protein thermal stability is evaluated by recording the changes in the heat capacity of proteins as temperature changes.