Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Biophysical Characterization and Stability of Modified IgG1 Antibodies with Different Hexamerization Propensities.

Journal of pharmaceutical sciences - 1 Jun 2022

van Kampen Muriel D, Kuipers-De Wilt Leonie H A M, van Egmond Mariëlle L, Reinders-Blankert Petra, van den Bremer Ewald T J, Wang Guanbo, Heck Albert J R, Parren Paul W H I, Beurskens Frank J, Schuurman Janine, de Jong Rob N

Abstract excerpt

The hexamerization of natural, human IgG antibodies after cell surface antigen binding can induce activation of the classical complement pathway. Mutations stimulating Fc domain-mediated hexamerization can potentiate complement activation and induce the clustering of cell surface receptors, a finding that was applied to different clinically investigated antibody therapeutics. Here, we biophysically characterized...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Complement Activation
Share to Immunoglobulin G

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Stability

Source

Identifiers

PMID: 35235843
DOI: 10.1016/j.xphs.2022.02.016

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Biophysical Characterization and Stability of Modified IgG1 Antibodies with Different Hexamerization Propensities.PMID 35235843Read ↗

Monovalent IgG4 molecules: immunoglobulin Fc mutations that result in a monomeric structure.Semantic proximity Read ↗

Molecular Basis of Assembly and Activation of Complement Component C1 in Complex with Immunoglobulin G1 and Antigen.Semantic proximity Read ↗

A Novel Platform for the Potentiation of Therapeutic Antibodies Based on Antigen-Dependent Formation of IgG Hexamers at the Cell Surface.Semantic proximity Read ↗

Electrostatic interactions modulate the differential aggregation propensities of IgG1 and IgG4P antibodies and inform charged residue substitutions for improved developabilitySemantic proximity Read ↗

Mutational analysis of domain antibodies reveals aggregation hotspots within and near the complementarity determining regions.Semantic proximity Read ↗

Mitigation of reversible self-association and viscosity in a human IgG1 monoclonal antibody by rational, structure-guided Fv engineeringSemantic proximity Read ↗

Computational design of monomeric Fc variants with distinct pH-responsive FcRn-binding profilesSemantic proximity Read ↗

Stability engineering of the human antibody repertoireSemantic proximity Read ↗

The role of amino acid sequence in the self-association of therapeutic monoclonal antibodies: insights from coarse-grained modeling.Semantic proximity Read ↗

An "Fc-Silenced" IgG1 Format With Extended Half-Life Designed for Improved Stability.Semantic proximity Read ↗

Mutation of Y407 in the CH3 domain dramatically alters glycosylation and structure of human IgG.Semantic proximity Read ↗

Stellabody: A novel hexamer-promoting mutation for improved IgG potency.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.