ArticleBiotechnology and bioengineering2010
IgG-single chain Fv fusion protein therapeutic for Alzheimer's disease: Expression in CHO cells and pharmacokinetics and brain delivery in the rhesus monkey.
Article in Biotechnology and bioengineering, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 46 citations in OpenAlex.
- Antibody-Based Biologics for CNS Disorders.Antibodies (Basel, Switzerland) · 2026Review
- Drug delivery strategies to cross the blood-brain barrier in Alzheimer's disease: a comprehensive review on three promising strategies.The journal of prevention of Alzheimer's disease · 2025Review
- Emerging trends in virus and virus-like particle gene therapy delivery to the brain.Molecular therapy. Nucleic acids · 2024Review
- IgG-like bispecific antibodies with potent and synergistic neutralization against circulating SARS-CoV-2 variants of concern.Nature communications · 2022Article
- Engineering antibody and protein therapeutics to cross the blood-brain barrier.Antibody therapeutics · 2022Review
- IgG Fusion Proteins for Brain Delivery of Biologics via Blood-Brain Barrier Receptor-Mediated Transport.Pharmaceutics · 2022Review
- Intramuscular injection of vectorized-scFvMC1 reduces pathological tau in two different tau transgenic models.Acta neuropathologica communications · 2020Article
- Review of Current Strategies for Delivering Alzheimer's Disease Drugs across the Blood-Brain Barrier.International journal of molecular sciences · 2019Review
- Pharmacokinetic parameters and mechanism of action of an efficient anti-Aβ single chain antibody fragment.PloS one · 2019Article
- Transcytosis to Cross the Blood Brain Barrier, New Advancements and Challenges.Frontiers in neuroscience · 2018Review
- High-affinity Anticalins with aggregation-blocking activity directed against the Alzheimer β-amyloid peptide.The Biochemical journal · 2016Article
- Targeting receptor-mediated transport for delivery of biologics across the blood-brain barrier.Annual review of pharmacology and toxicology · 2015Review
- Agile delivery of protein therapeutics to CNS.Journal of controlled release : official journal of the Controlled Release Society · 2014Review
- Single-chain fragment variable passive immunotherapies for neurodegenerative diseases.International journal of molecular sciences · 2013Review
- Genomics of Dementia: APOE- and CYP2D6-Related Pharmacogenetics.International journal of Alzheimer's disease · 2012Article
- Receptor-mediated abeta amyloid antibody targeting to Alzheimer's disease mouse brain.Molecular pharmaceutics · 2011Article
- Article
- Biologic TNFα-inhibitors that cross the human blood-brain barrier.Bioengineered bugsArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Monoclonal antibodies (MAb) directed against the Abeta amyloid peptide of Alzheimer's disease (AD) are potential new therapies for AD, since these antibodies disaggregate brain amyloid plaque. However, the MAb is not transported across the blood-brain barrier (BBB). To enable BBB transport, a single chain Fv (ScFv) antibody against the Abeta peptide of AD was re-engineered as a fusion protein with the MAb against the human insulin receptor (HIR). The HIRMAb acts as a molecular Trojan horse to ferry the ScFv therapeutic antibody across the BBB. Chinese hamster ovary (CHO) cells were stably transfected with a tandem vector encoding the heavy and light chains of the HIRMAb-ScFv fusion protein. A high secreting line was isolated following methotrexate amplification and dilutional cloning. The HIRMAb-ScFv fusion protein in conditioned serum-free medium was purified by protein A affinity chromatography. The fusion protein was stable as a liquid formulation, and retained high-affinity binding of both the HIR and the Abeta amyloid peptide. The HIRMAb-ScFv fusion protein was radiolabeled with the (125)I-Bolton-Hunter reagent, followed by measurement of the pharmacokinetics of plasma clearance and brain uptake in the adult Rhesus monkey. The HIRMAb-ScFv fusion protein was rapidly cleared from plasma and was transported across the primate BBB in vivo. In conclusion, the HIRMAb-ScFv fusion protein is a new class of antibody-based therapeutic for AD that has been specifically engineered to cross the human BBB.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.