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Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
Published on: May 13, 2010
'Amytrapper', a Novel Immobilized Sepharose API Matrix, Removes Amyloid-β from Circulation in vitro
Omkar Gandbhir1, Pazhani Sundaram1
1Recombinant Technologies LLC, Cheshire, CT, USA.
Journal of Alzheimer'S Disease Reports
|March 8, 2019
Summary
A novel Amytrap peptide, immobilized on sepharose as Amytrapper, effectively removes amyloid-beta (Aβ) from circulation. This demonstrates a potential new therapy for Alzheimer's disease (AD) by reducing Aβ accumulation.
Area of Science:
- Neuroscience
- Biochemistry
- Biotechnology
Background:
- Alzheimer's disease (AD) is a leading cause of dementia, characterized by amyloid-beta (Aβ) accumulation.
- Current therapies targeting Aβ production have limited success, necessitating novel approaches.
- Recombinant Technologies LLC (RTL) developed Amytrap peptide to clear Aβ from circulation.
Purpose of the Study:
- To develop and validate a prototype device, 'Amytrapper', for extracorporeal Aβ clearance.
- To assess the efficacy and specificity of Amytrapper in removing Aβ.
Main Methods:
- The Amytrap peptide (active pharmaceutical ingredient) was conjugated to a sepharose matrix using click chemistry.
- Amytrapper's ability to remove Aβ42 from media, sera, and plasma was tested.
- Binding specificity was confirmed through pre-blocking, SDS-PAGE, and quantifying bound/unbound Aβ42.
Main Results:
- Amytrapper successfully removed Aβ42 from spiked media and biological samples (sera, plasma).
- Binding was specific, as demonstrated by competitive inhibition assays and SDS-PAGE analysis.
- The study provides proof of concept for the Amytrapper device design.
Conclusions:
- Extracorporeal clearance of Aβ42 using Amytrapper is a viable strategy for managing amyloid accumulation in Alzheimer's disease.
- Amytrapper represents a potential new therapeutic modality for disease modification in AD.
Keywords:
Alzheimer’s diseaseAlzheimer’s therapyAmytrapperamyloidamyloid-β peptidesextracorporealplasmapheresis
