Article

Structural conservation and expanded functionality of hyper-stable human serum albumin variants

2026-04-11

Abstract excerpt

Human serum albumin (hSA) is the most abundant protein in human plasma, and its pharmacological properties, such as long plasma half-life mediated by the neonatal Fc receptor (FcRn) and its ability to bind endogenous and exogenous molecules, make it attractive for biotechnological applications. Currently, most wild type (WT) SAs are derived from human or bovine serum or produced in yeast and mammalian cells. Altho...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 944e769a-165a-5ea3-af9e-cdbf5cdb1fd9
DOI: 10.64898/2026.04.10.717531

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Structural conservation and expanded functionality of hyper-stable human serum albumin variantsDOI 10.64898/2026.04.10.717531Read

Stable mammalian serum albumins designed for bacterial expressionSemantic 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

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

Crystal structure of human serum albumin in complex with megabody reveals unique human and murine cross‐reactive binding siteSemantic proximity Read

Structural insights into neonatal Fc receptor-based recycling mechanisms.Semantic proximity Read

Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor.Semantic proximity Read

Human serum albumin isoforms: Genetic and molecular aspects and functional consequencesSemantic proximity Read

Stability engineering of the human antibody repertoireSemantic proximity Read

Direct demonstration of a neonatal Fc receptor (FcRn)-driven endosomal sorting pathway for cellular recycling of albumin.Semantic proximity Read

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

Hemoglobin Variants as Targets for Stabilizing DrugsSemantic proximity Read

Fusion to a highly stable consensus albumin binding domain allows for tunable pharmacokineticsSemantic proximity Read