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- W2911498045 abstract "Protein stability, particularly antibody stability, can be determined by calorimetry without restrictions on buffers, excipients, and detergents. This native assay works equally well for novel biotherapeutics some of which are bispecific antibodies, biosimilars, and modified antibodies including antibody drug conjugates (ADC). For this ADC example, maytansine bound to trastuzumab was prepared using two different methods: on-bead and off-bead. The DSC thermogram was able to capture and quantify the potential differences with regards to stability while ITC dissected the binding to the HER2 protein into its’ enthalpic and entropic contributions all while providing stoichiometry, which could have relevance to bioavailability." @default.
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- W2911498045 date "2019-02-01" @default.
- W2911498045 modified "2023-10-14" @default.
- W2911498045 title "Native Quantitative Determination of Antibody-Drug Conjugate Affinity and Stability" @default.
- W2911498045 doi "https://doi.org/10.1016/j.bpj.2018.11.1067" @default.
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