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• W2037441461 abstract "The susceptibility of monoclonal antibodies (mAbs) to undergo cold denaturation remains unexplored. In this study, the phenomenon of cold denaturation was investigated for a mAb, mAb1, through thermodynamic and spectroscopic analyses. Tryptophan fluorescence and circular dichroism (CD) spectra were recorded for the guanidine hydrochloride (GuHCl)-induced unfolding of mAb1 at pH 6.3 at temperatures ranging from -5 to 50°C. A three-state unfolding model incorporating the linear extrapolation method was fit to the fluorescence data to obtain an apparent free energy of unfolding, ΔGu, at each temperature. CD studies revealed that mAb1 exhibited polyproline II helical structure at low temperatures and at high GuHCl concentrations. The Gibbs-Helmholtz expression fit to the ΔGu versus temperature data from fluorescence gave a ΔCp of 8.0 kcal mol-1 K-1, a maximum apparent stability of 23.7 kcal mol-1 at 18°C, and an apparent cold denaturation temperature (TCD) of -23°C. ΔGu values for another mAb (mAb2) with a similar framework exhibited less stability at low temperatures, suggesting a depressed protein stability curve and a higher relative TCD. Direct experimental evidence of the susceptibility of mAb1 and mAb2 to undergo cold denaturation in the absence of denaturant was confirmed at pH 2.5. Thus, mAbs have a potential to undergo cold denaturation at storage temperatures near -20°C (pH 6.3), and this potential needs to be evaluated independently for individual mAbs." @default.
• W2037441461 created "2016-06-24" @default.
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• W2037441461 date "2010-01-01" @default.
• W2037441461 modified "2023-09-26" @default.
• W2037441461 title "Cold denaturation of monoclonal antibodies" @default.
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• W2037441461 doi "https://doi.org/10.4161/mabs.2.1.10787" @default.
• W2037441461 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2828577" @default.
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