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• W2340568519 endingPage "xiii" @default.
• W2340568519 startingPage "vii" @default.
• W2340568519 abstract "Bispecific antibodies (bsAbs) combine the antigen specificities of two distinct Abs and demonstrate therapeutic promise based on novel mechanisms of action. Among the many platforms for creating bsAbs, controlled Fab-arm exchange (cFAE) has proven useful based on minimal changes to native Ab structure and the simplicity with which bsAbs can be formed from two parental Abs. Despite a published protocol for cFAE and its widespread use in the pharmaceutical industry, the reaction mechanism has not been determined. Knowledge of the mechanism could lead to improved yields of bsAb at faster rates as well as foster adoption of process control. In this work, a combination of Förster resonance energy transfer (FRET), nonreducing SDS-PAGE, and strategic mutation of the Ab hinge region was employed to identify and characterize the individual steps of cFAE. Fluorescence correlation spectroscopy (FCS) was used to determine the affinity of parental (homodimer) and bispecific (heterodimer) interactions within the CH3 domain, further clarifying the thermodynamic basis for bsAb formation. The result is a clear sequence of events with rate constants that vary with experimental conditions, where dissociation of the K409R parental Ab into half-Ab controls the rate of the reaction." @default.
• W2340568519 created "2016-06-24" @default.
• W2340568519 creator A5039190287 @default.
• W2340568519 creator A5069729938 @default.
• W2340568519 date "2016-06-01" @default.
• W2340568519 modified "2023-09-24" @default.
• W2340568519 title "Editorial overview: Special section: New concepts in antibody therapeutics: What's in store for antibody therapy?" @default.
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• W2340568519 doi "https://doi.org/10.1016/j.coi.2016.04.001" @default.
• W2340568519 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27083411" @default.
• W2340568519 hasPublicationYear "2016" @default.
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