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An engineered human Fc domain that behaves like a pH-toggle switch for ultra-long circulation persis...

An engineered human Fc domain that behaves like a pH-toggle switch for ultra-long circulation persis...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_84d23b07351d4847b7e49dca2fbb568c

An engineered human Fc domain that behaves like a pH-toggle switch for ultra-long circulation persistence

About this item

Full title

An engineered human Fc domain that behaves like a pH-toggle switch for ultra-long circulation persistence

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2019-11, Vol.10 (1), p.5031-11, Article 5031

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The pharmacokinetic properties of antibodies are largely dictated by the pH-dependent binding of the IgG fragment crystallizable (Fc) domain to the human neonatal Fc receptor (hFcRn). Engineered Fc domains that confer a longer circulation half-life by virtue of more favorable pH-dependent binding to hFcRn are of great therapeutic interest. Here we...

Alternative Titles

Full title

An engineered human Fc domain that behaves like a pH-toggle switch for ultra-long circulation persistence

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_84d23b07351d4847b7e49dca2fbb568c

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_84d23b07351d4847b7e49dca2fbb568c

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-019-13108-2

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