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Article

Tuning the serum persistence of human serum albumin domain III:diabody fusion proteins.

Protein engineering, design & selection : PEDS - 1 Oct 2010

Kenanova Vania E, Olafsen Tove, Salazar Felix B, Williams Lawrence E, Knowles Scott, Wu Anna M

Abstract excerpt

The long circulation persistence of human serum albumin (HSA) is enabled by its domain III (DIII) interaction with the neonatal Fc receptor (FcRn). A protein scaffold based on HSA DIII was designed. To modify the serum half life of the scaffold, residues H535, H510, and H464 were individually mutated to alanine. HSA DIII wild type (WT) and variants were fused to the anti-carcinoembryonic antigen (CEA) T84.66...

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

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Source

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Identifiers

PMID: 20802234
DOI: 10.1093/protein/gzq054
PMCID: PMC2935312

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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