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

Extending Half-life by Indirect Targeting of the Neonatal Fc Receptor (FcRn) Using a Minimal Albumin Binding Domain

7 Dec 2010

Abstract excerpt

The therapeutic and diagnostic efficiency of engineered small proteins, peptides, and chemical drug candidates is hampered by short in vivo serum half-life. Thus, strategies to tailor their biodistribution and serum persistence are highly needed. An attractive approach is to take advantage of the exceptionally long circulation half-life of serum albumin or IgG, which is attributed to a pH-dependent interaction...

Read the complete abstract on PubMed

Topics

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

Share to Blood groups and transfusion
Share to Glycosylation and Glycoproteins Research
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 21138843
DOI: 10.1074/jbc.m110.164848

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 23 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Extending Half-life by Indirect Targeting of the Neonatal Fc Receptor (FcRn) Using a Minimal Albumin Binding DomainPMID 21138843Read ↗

Fusion of a Short Peptide that Binds Immunoglobulin G to a Recombinant Protein Substantially Increases Its Plasma Half-Life in MiceSemantic proximity Read ↗

Neonatal Fc receptor (FcRn): a novel target for therapeutic antibodies and antibody engineering.Semantic proximity Read ↗

Selection of IgG Variants with Increased FcRn Binding Using Random and Directed Mutagenesis: Impact on Effector FunctionsSemantic proximity Read ↗

Serum albumin‐binding V H Hs with variable pH sensitivities enable tailored half‐life extension of biologicsSemantic proximity Read ↗

Half-life extension using serum albumin-binding DARPin® domainsSemantic proximity Read ↗

Engineered human IgG antibodies with longer serum half-lives in primates.Semantic proximity Read ↗

A novel in vitro assay to predict neonatal Fc receptor-mediated human IgG half-lifeSemantic proximity Read ↗

Evaluation of an FcRn affinity chromatographic method for IgG1-type antibodies and evaluation of IgG variants.Semantic proximity Read ↗

Engineered human FcγRIIa fusion: A novel strategy to extend serum half-life of therapeutic proteins.Semantic proximity Read ↗

An Fc variant with two mutations confers prolonged serum half-life and enhanced effector functions on IgG antibodies.Semantic proximity Read ↗

Interaction with Both Domain I and III of Albumin Is Required for Optimal pH-dependent Binding to the Neonatal Fc Receptor (FcRn)Semantic proximity Read ↗

Enhanced half-life of genetically engineered human IgG1 antibodies in a humanized FcRn mouse model: potential application in humorally mediated autoimmune diseaseSemantic proximity Read ↗

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