HSA Domain III as a protein scaffold with defined serum pharmacokinetics

V Kenanova, T Olafsen, F Bergara, A Wu - 2009 - Soc Nuclear Med
1582 Objectives Our objective is to generate a protein scaffold of small molecular size,
controlled serum persistence and architecture suitable for modification. When attached to …

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

VE Kenanova, T Olafsen, FB Salazar… - … , Design & Selection, 2010 - academic.oup.com
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 …

Serum albumin‐binding VHHs with variable pH sensitivities enable tailored half‐life extension of biologics

H van Faassen, S Ryan, KA Henry… - The FASEB …, 2020 - Wiley Online Library
Prolonged serum half‐life is required for the efficacy of most protein therapeutics. One
strategy for half‐life extension is to exploit the long circulating half‐life of serum albumin by …

Biodistribution and tumor imaging of an anti-CEA single-chain antibody–albumin fusion protein

PJ Yazaki, T Kassa, C Cheung, DM Crow… - Nuclear medicine and …, 2008 - Elsevier
Albumin fusion proteins have demonstrated the ability to prolong the in vivo half-life of small
therapeutic proteins/peptides in the circulation and thereby potentially increase their …

Structural basis of serum albumin recognition by SL335, an antibody Fab extending the serum half-life of protein therapeutics

SY Cho, J Han, SH Cha, S Yoon - Biochemical and Biophysical Research …, 2020 - Elsevier
Human serum albumin (HSA) has been used to extend the serum half-lives of various
protein therapeutics through genetic fusion because HSA exhibits an exceptionally long …

Engineered human FcγRIIa fusion: A novel strategy to extend serum half‐life of therapeutic proteins

M Jo, S Ko, B Hwang, SW Min, JY Ha… - Biotechnology and …, 2020 - Wiley Online Library
The immunoglobulin G (IgG) molecule has a long circulating serum half‐life (~ 3 weeks)
through pH‐dependent FcRn binding‐mediated recycling. To hijack the intracellular …

PET-guided evaluation and optimization of internalized antibody–drug conjugates targeting erythropoietin-producing hepatoma A2 receptor

O Jacobson, Q Li, H Chen, G Niu… - Journal of Nuclear …, 2017 - Soc Nuclear Med
The erythropoietin-producing hepatoma A2 receptor (EphA2) is a tyrosine kinase
overexpressed by tumor stroma and cancer cells. A high expression level of EphA2 predicts …

Designer genes: recombinant antibody fragments for biological imaging

AM Wu, PJ Yazaki - The Quarterly Journal of Nuclear Medicine …, 2000 - search.proquest.com
Monoclonal antibodies (MAbs), with high specificy and high affinity for their target antigens,
can be utilized for delivery of agents such as radionuclides, enzymes, drugs, or toxins in …

Self-Assembling and DisAssembling Bispecific Antibodies for Curative 2-step Pretargeted Radioimmunotherapy

B Santich, S Cheal, M Ahmed, M McDevitt, O Ouerfelli… - 2020 - Soc Nuclear Med
34 Introduction: Conventional pre-targeted radioimmunotherapy (PRIT) has relied on long
incubations between targeting and payload delivery (2-step) or synthetic clearing agents (3 …

[PDF][PDF] Crystal structure of an HSA/FcRn complex reveals recycling by competitive mimicry of HSA ligands at a pH-dependent hydrophobic interface

MM Schmidt, SA Townson, AJ Andreucci, BM King… - Structure, 2013 - cell.com
The long circulating half-life of serum albumin, the most abundant protein in mammalian
plasma, derives from pH-dependent endosomal salvage from degradation, mediated by the …