Peptides for Alzheimer's Disease Research


About Alzheimer's Disease

Alzheimer's Disease (AD) is a neurodegenerative disorder that progressively damages brain cells, leading to memory loss, cognitive decline, and eventually death. Most commonly diagnosed after the age of 65, Alzheimer's also affects younger individuals, with about 5% of patients suffering from early-onset Alzheimer's Disease. Despite extensive research, the exact mechanisms causing Alzheimer's remain unclear. However, several hypotheses exist to explain its development.

One hypothesis focuses on the hyperphosphorylation of tau protein, while another centers around the buildup of amyloid plaques in the brain. These plaques are primarily composed of amyloid beta (Aβ) peptides, which are also implicated in other protein misfolding diseases, such as prion disorders. Understanding the role of peptides in Alzheimer's disease is critical to advancing potential treatments and therapies.


Role of Amyloid Beta Peptide in Alzheimer's Disease

Amyloid Beta (Aβ), also known as Beta Amyloid A4, plays a pivotal role in Alzheimer's disease pathology:

  • Beta Amyloid A4 peptide (also referred to as Aβ, Abeta, Amyloid Beta) serves several functions in a healthy brain, such as activating kinases and regulating cholesterol transport.
  • The accumulation of amyloid plaques, primarily composed of Aβ peptides, is a key pathological hallmark of Alzheimer's disease.
  • Aβ peptides arise from the amyloid precursor protein (APP), undergoing proteolytic processing through β- and γ-secretases.
  • These peptides vary in length (up to 43 amino acids), and certain isoforms, particularly Aβ(1-42) and Aβ(1-43), are highly prone to aggregation.
  • A pathological increase in β/γ-secretase activities and a reduced clearance rate of Aβ peptides can result in their accumulation in the brain, contributing to the formation of toxic oligomers, fibrils, and plaques.
  • These amyloid beta aggregates disturb the neuronal network and are believed to exert neurotoxic effects, leading to the cognitive and behavioral impairments observed in Alzheimer's patients.
  • Despite years of research, the exact biochemical pathways driving the neurotoxic effects of Aβ peptides are still not fully understood, making Alzheimer's disease research a critical area of focus for peptide scientists.


JPT's Peptide Tools for Alzheimer's Research

Amyloid Beta Peptides for Alzheimer's Research

At JPT, we provide a comprehensive collection of Amyloid Beta (Aβ) peptides for studying Alzheimer's disease. Our peptide portfolio includes both various lengths of Aβ peptides and point-mutated versions of Aβ(1-42), known to be associated with familial forms of Alzheimer's. These peptides are delivered as HFIP-films (hexafluoroisopropanol) to eliminate unwanted secondary structures and any pre-existing oligomers or polymers, ensuring maximum experimental accuracy.

Researchers focusing on Alzheimer’s peptide studies can benefit from the high purity and customization of these peptides for in vitro and in vivo Alzheimer's research.

Custom Peptide Synthesis for Alzheimer's Disease Studies

Custom peptides synthesis for Alzheimer's play an essential role in advancing Alzheimer's studies by enabling scientists to create specific peptides for their unique research needs. JPT is renowned for our Custom Peptide Synthesis services, offering:

  • Over 99% success rate in peptide synthesis, optimizing the process for each specific peptide sequence.
  • Tailored solutions for Alzheimer's peptide research, with strict quality control and regulated processes to ensure consistency and accuracy.
  • A dedicated team of peptide experts, ensuring your peptides meet the highest standards required for Alzheimer’s disease studies.

Whether you are looking for standard Aβ peptides or complex, modified peptides for Alzheimer's research, JPT’s synthesis services provide the best tools to accelerate your experiments.


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References

References


  • 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

Testimonial

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

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