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. 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.

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 Alzheimer's Peptide Tools

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.

Custom Peptides

We are the experts for peptide synthesis with highest quality optimized for many applications. Our peptide synthesis service has a very high success rate (over 99%) as we optimize the appropriate peptide synthesis method for each peptide.
If you would like to order a quality peptide synthesis using regulated processes, choose JPT!




  • Systemic inflammation elevates cytosolic prolyl oligopeptidase protein expression but not peptidase activity in the cerebral cortices of familial Alzheimer`s disease modeling mice
    Puris et al., Brain Disorders (2022) 
  • Enhanced ion mobility resolution of Abeta isomers from human brain using high‑resolution demultiplexing software
    Mukherjee et al., Analytical and Bioanalytical Chemistry (2022)
  • A novel D-amino acid peptide with therapeutic potential (ISAD1) inhibits aggregation of neurotoxic disease-relevant mutant Tau and prevents Tau toxicity in vitro
    Isabelle Aillaud et al., Alzheimer's Research & Therapy, (2022)
  • A Comparative Study of the Effects of Aducanumab and Scanning Ultrasound on Amyloid Plaques and Behavior in the APP23 Mouse Model of Alzheimer Disease
    Gerhard Leinenga et al., bioRxiv (2020) - PMID: n.a.
  • Citrullination of Amyloid-β Peptides in Alzheimer’s Disease
    Soumya Mukherjee et al., ACS Chem Neurosci, (2021)
  • Lithium Ions Display Weak Interaction With Amyloid-Beta (Aβ) Peptides And Have Minor Effects On Their Aggregation
    Elina Berntsson et al., bioRxiv (2020) - PMID: n.a.
  • Analyzing Microglial‑Associated Aβ in Alzheimer’s Disease Transgenic Mice With a Novel Mid‑Domain Aβ‑Antibody
    Kristi Henjum et al., Scientific Reports (2020) - PMID: 32601313
  • In Situ Structural Characterization of Early Amyloid Aggregates in Alzheimer’s Disease Transgenic Mice And Octodon Degus
    Núria Benseny-Cases et al., Scientific Reports (2020) - PMID: 32246090
  • Long‑term cafeine treatment of Alzheimer mouse models ameliorates behavioural defcits and neuron loss and promotes cellular and molecular markers of neurogenesis
    Martina Stazi et al., Cellular and Molecular Life Science, (2021)
  • 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) 
  • 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 A2T Modulates Kinetic and Thermodynamic Properties of Amyloid-β (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
  • Effect of Poly(propylene imine) Glycodendrimers on β-Amyloid Aggregation in Vitro and in APP/PS1 Transgenic Mice, as a Model of Brain Amyloid Deposition and Alzheimer’s Disease
    Klementieva et al., Biomacromolecules (2013) - PMID: 24004423
  • Nanoparticulate Flurbiprofen Reduces Amyloid-β42 Generation in an in Vitro Blood-Brain Barrier Model
    Meister et al., Alzheimers Research & Therapy (2013) - PMID: 24280275
  • The Amyloid-β Oligomer Count in Cerebrospinal Fluid is a Biomarker for Alzheimer's Disease
    Wang-Dietrich et al., Journal of Alzheimer's Disease (2013) - PMID: 23313925
  • DNA Beta-Amyloid1-42 Trimer Immunization for Alzheimer Disease in a Wild-Type Mouse Model
    Lambracht-Washington et al., JAMA, (2009) - PMID: 19861672



“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

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