Peptide Tools to Study Alzheimer's Disease
About Alzheimer's Disease
Alzheimer's Disease is a neurodegenerative disease that typically begins after the age of 65 years and progresses until death. 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.
Amyloid Beta Peptide
- 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
JPT's Peptide Tools to Study Alzheimer:
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.
Selected Alzheimer Related References
"Competitive Mirror Image Phage Display Derived Peptide Modulates Amyloid Beta Aggregation and Toxicity"
Rudolph et al., PLoS One. (2016) - PMID: 26840229
"Inhibition of the Cardiac Na+ Channel α-subunit Nav1. 5 by Propofol and Dexmedetomidine"
Stoetzer et al., Naunyn Schmiedebergs Arch Pharmacol. - PMID: 26667357
"η-Secretase Processing of APP Inhibits Neuronal Activity in the Hippocampus"
Willem et al., Nature (2015) - PMID: 26322584
"Aβ-42 lowering Agents From the Marine-Derived Fungus Dichotomomyces Cejpii"
Harms et al., Steroids. (2015) – PMID: 26440473
"Hybridization of an Aβ-specific Antibody Fragment with Aminopyrazole-based β Sheet Ligands Displays Striking Enhancement of Target Affinity"
Hellmert et al., Org. Biomol. Chem. (2015)
"Structural Differences of Amyloid-β fibrils Revealed by Antibodies From Phage Display"
Droste et al., BMC Biotechnol. (2015) - PMID: 26084577
"Neprilysin Deficiency Alters the Neuropathological and Behavioral Phenotype in the 5XFAD Mouse Model of Alzheimer's Disease"
Huettenrauch et al., J Alzheimers Dis. (2014) - PMID: 25408216
"Monoclonal Antibodies Against Ab42 Fibrils Distinguish Multiple Aggregation State Polymorphisms in vitro and in Alzheimer's Disease Brain"
Hatami et al., J. Biol. Chem. (2014) - PMID: 25281743
"The Alzheimer Disease Protective Mutation Ala2Thr Modulates Kinetic and Thermodynamic Properties of Aβ Aggregation"
Benilova et al., J Biol Chem. (2014) - PMID: 25253695
"Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4"
Argyri et al., J. Biol. Chem. (2014) - PMID: 24644280
Selected Alzheimer Related Testimonial
“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)
More application notes