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Article

Engineering human IgG1 affinity to human neonatal Fc receptor: impact of affinity improvement on pharmacokinetics in primates.

Journal of immunology (Baltimore, Md. : 1950) - 15 Jun 2009

Yeung Yik Andy, Leabman Maya K, Marvin Jonathan S, Qiu Julia, Adams Camellia W, Lien Samantha, Starovasnik Melissa A, Lowman Henry B

Abstract excerpt

The pH-dependent binding of Igs to the neonatal FcR (FcRn) plays a critical role in the in vivo homeostasis of IgGs. Modulating the interaction between Fc and FcRn through protein engineering is one method for improving the pharmacokinetics of therapeutic Abs. Recent studies disputed the direct relationship between increasing FcRn affinity and improved pharmacokinetic properties. In this work, we studied the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 19494290
DOI: 10.4049/jimmunol.0804182

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Engineering human IgG1 affinity to human neonatal Fc receptor: impact of affinity improvement on pharmacokinetics in primates.PMID 19494290Read ↗

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Monoclonal Antibody Engineering and Design to Modulate FcRn Activities: A Comprehensive ReviewSemantic proximity Read ↗

Changes in complementarity-determining regions significantly alter IgG binding to the neonatal Fc receptor (FcRn) and pharmacokinetics.Semantic proximity Read ↗

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