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presence of polysorbate 20 and 80 (PS20 and PS80,
respectively), which are common surfactants for
the majority of mAb formulations, but preclude the
analysis by orthogonal fl uorescence methods such as
DSF assays (will be reported elsewhere).
Representative data for the thermal unfolding
experiments by µDSC and nanoDSF are shown in
Figure 1. For nanoDSF, samples were measured in
triplicates, while samples where measured only
once with µDSC to save time and sample material.
Figure 2: (A) Comparison of T
m
1 and T
m
2 values determined by nanoDSF (n=3) and µDSC (n=1). nanoDSF data points represent average values. Error
bars are smaller than symbol sizes (s.d. <0.1 °C for all measured samples). (B) Comparison of the time- and sample requirements of nanoDSF and µDSC
for a formulation screen involving 48 diff erent samples. (C) Summary of benefi ts and limitations of µDSC and nanoDSF for the determination of protein
thermal stability. Protein concentration ranges are given for mAb solutions.
