Alzheimer's Disease is a neurodegenerative disease that typically begins after the age of 65 years and progresses until death. However, early-onset Alzheimer’s affects younger people, around 5% of people with Alzheimer’s are under 65.
Although the mechanisms are poorly understood, several hypotheses on the cause of Alzheimer's Disease exist. One of them is that an abnormally hyperphosphorylated tau protein initiates the disease. Another hypothesis states that the main pathogenic factor in Alzheimer's disease are amyloid plaques forming in the brain. Amyloid plaques are composed of regularly ordered amyloid fibers, a peptide fold also associated with protein misfolding diseases such as prion diseases.
- Beta Amyloid A4 peptide (synonyms are Aβ, Abeta, Amyloid Beta)
- Several functions in healthy organisms, e.g. activation of kinases and cholesterol transport regulation
- Main component of amyloid plaques
- Arise from proteolytic processing of amyloid precursor protein (APP) involving sequential cleavages by ß- and γ-secretases
- Represent a mixture of peptides of different lengths (up to 43 amino acids)
- Pathological increase of ß/γ-secretase activities and diminished clearance rate initiate accumulation and aggregation of amyloid-ß peptides in the brain tissue of Alzheimer patients
- The two isoforms Aß(1-42) and Aß(1-43) tend to aggregate
- Resulting amyloid-ß peptide oligomers, fibrils and plaques disturb the neuronal network and show strong neurotoxic effects
- The exact biochemical pathways underlying the pathologic effects of amyloid-ß peptides are not quite understood
Amyloid beta Peptides
JPT provides a broad selection of chemically synthesized amyloid-ß peptides for Alzheimer's disease research. We supply Abeta peptides of different lengths and point-mutated versions of Aß(1-42) which are known to be related to the familial forms of Alzheimer`s disease. They are provided as HFIP-films (HFIP = hexafluoroisopropanol) which removes any unwanted secondary peptide structure and pre-existing oligomeric/polymeric forms.
"Alzheimer's Disease Phenotype or Inflammatory Insult Does Not Alter Function of L-Type Amino Acid Transporter 1 in Mouse Blood-Brain Barrier and Primary Astrocytes"
Gynther et al., Pharmaceutical Research (2019)
"Poly(propylene imine) Dendrimers With Histidine-Maltose Shell as Novel Type of Nanoparticles for Synapse and Memory Protection"
Aso et al., Nanomedicine: Nanotechnology, Biology and Medicine (2019)
"The Metalloprotease ADAMTS4 Generates N-truncated Aβ4-x Species and Marks Oligodendrocytes as a Source of Amyloidogenic Peptides in Alzheimer's Disease"
Walter et al., Acta Neuropathologica (2018)
"Amyloid-peptide β 42 Enhances the Oligomerization and Neurotoxicity of apoE4: The C-terminal Residues Leu279, Lys282 and Gln284 Modulate the Structural and Functional Properties of apoE4 I"
Dafnis et al., Neuroscience (2018)
"Synchrotron-Based µFTIR Study on the Effect of Alzheimer´s Aβ Amorphous and Fibrillar Aggregates on PC12 Cells"
Benseny-Cases et al., Analytical Chemistry (2018) - PMID: 29359921
“Our group focuses on the in vitro study of risk factors in Alzheimer’s disease and, as we experienced that the in-house expression and production of the amyloid beta peptide is notoriously difficult, we are continuously dependent on a high quality supply of a large variety of these peptides from commercial source. We started our collaboration with JPT with their request to test a range of their peptides for the ability to produce toxic oligomers and fibrillar networks and were impressed by the rapid supply of a very wide range of high purity peptides with excellent fibril forming properties and toxicity profiles. JPT has shown real valuable know-how and experience in the field of peptide synthesis by their ability to generate high quality preparations of amyloid beta peptide variants which are known for their difficulty to handle.”
Kerensa Broersen, Assistant Prof., Nanobiophysics Group, University of Twente, Enschede, The Netherlands
Synthetic Amyloid Beta Peptides Aid Alzheimer Investigation
Vandersteen et al., Application Note (2013)
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