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• W2057362015 abstract "Efforts have been made to extend the biological half-life of monoclonal antibody drugs (mAbs) by increasing the affinity of mAb-neonatal Fc receptor (FcRn) binding; however, mixed results have been reported. One possible reason for a poor correlation between the equilibrium affinity of mAb-FcRn binding and mAb systemic pharmacokinetics is that the timecourse of endosomal transit is too brief to allow binding to reach equilibrium. In the present work, a new physiologically based pharmacokinetic (PBPK) model has been developed to approximate the pH and time-dependent endosomal trafficking of immunoglobulin G (IgG). In this model, a catenary sub-model was utilized to describe the endosomal transit of IgG and the time dependencies in IgG-FcRn association and dissociation. The model performs as well as a previously published PBPK model, with assumed equilibrium kinetics of mAb-FcRn binding, in capturing the disposition profile of murine mAb from wild-type and FcRn knockout mice (catenary vs. equilibrium model: r (2), 0.971 vs. 0.978; median prediction error, 3.38% vs. 3.79%). Compared to the PBPK model with equilibrium binding, the present catenary PBPK model predicts much more moderate changes in half-life with altered FcRn binding. For example, for a 10-fold increase in binding affinity, the catenary model predicts <2.5-fold change in half-life compared to an ∼8-fold increase as predicted by the equilibrium model; for a 100-fold increase in binding affinity, the catenary model predicts ∼7-fold change in half-life compared to >70-fold increase as predicted by the equilibrium model. Predictions of the new catenary PBPK model are more consistent with experimental results in the published literature." @default.
• W2057362015 created "2016-06-24" @default.
• W2057362015 creator A5006940157 @default.
• W2057362015 creator A5020819058 @default.
• W2057362015 date "2012-09-07" @default.
• W2057362015 modified "2023-10-16" @default.
• W2057362015 title "Evaluation of a Catenary PBPK Model for Predicting the In Vivo Disposition of mAbs Engineered for High-Affinity Binding to FcRn" @default.
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• W2057362015 doi "https://doi.org/10.1208/s12248-012-9395-9" @default.
• W2057362015 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3475865" @default.
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