STABLE HETERODIMERIC ANTIBODY DESIGN WITH MUTATIONS IN THE Fc DOMAIN

The provided scaffolds have heavy chains that are asymmetric in the various domains (e.g. CH2 and CH3) to accomplish selectivity between the various Fc receptors involved in modulating effector function, beyond those achievable with a natural homodimeric (symmetric) Fc molecule, and increased stabil...

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Hauptverfasser: Dixit, Surjit Bhimarao, Poon, David Kai Yuen, Spreter Von Kreudenstein, Thomas, Lario, Paula Irene, Escobar-Cabrera, Eric
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creator Dixit, Surjit Bhimarao
Poon, David Kai Yuen
Spreter Von Kreudenstein, Thomas
Lario, Paula Irene
Escobar-Cabrera, Eric
description The provided scaffolds have heavy chains that are asymmetric in the various domains (e.g. CH2 and CH3) to accomplish selectivity between the various Fc receptors involved in modulating effector function, beyond those achievable with a natural homodimeric (symmetric) Fc molecule, and increased stability and purity of the resulting variant Fc heterodimers. These novel molecules comprise complexes of heterogeneous components designed to alter the natural way antibodies behave and that find use in therapeutics.
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subjects CHEMISTRY
INFORMATION AND COMMUNICATION TECHNOLOGY [ICT] SPECIALLY ADAPTEDFOR SPECIFIC APPLICATION FIELDS
METALLURGY
ORGANIC CHEMISTRY
PEPTIDES
PHYSICS
title STABLE HETERODIMERIC ANTIBODY DESIGN WITH MUTATIONS IN THE Fc DOMAIN
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