Explore our range of Amyloid Beta Peptides
Our extensive range of Amyloid Beta Peptides aims to support your research in understanding, targeting, and combating Alzheimer’s disease and other related neurodegenerative disorders. Whether you are conducting biochemical assays, investigating neuronal toxicity, or studying plaque formation, our products deliver unparalleled quality and reliability. Find our peptides here:
Can’t find what you’re looking for? You can also choose your own amyloid-beta peptide sequence, amount, and purity. Our Custom Peptide Synthesis team will guide you through the entire process.
Explore JPT Peptide Technologies’ peptide catalog if you’re interested in purchasing additional peptides!
Research areas and applications
Abeta peptides are central to the study of Alzheimer’s, from identifying early-stage oligomer formations to screening potential therapeutic compounds. By providing high-quality peptides, we empower researchers to further their understanding of the mechanisms behind the disease and develop potential treatments targeting these protein aggregates. Some of the most important research areas of these peptides are listed in the following:
- Neurodegeneration and Alzheimer’s studies: Used to investigate how their production, clearance, and misfolding contribute to Alzheimer’s disease and other neurodegenerative disorders.
- Aggregation and plaque formation studies: Serve as models for examining β-sheet formation and the progression from soluble oligomers to protofibrils and fibrils using NMR, AFM, cryo-EM, and related structural methods.
- Neurotoxicity studies: Applied to analyze how soluble beta amyloid oligomers disrupt synaptic signaling, induce oxidative stress, trigger apoptotic pathways, and impair neuronal membranes, contributing to Alzheimer’s pathology.
- Cerebrovascular studies: Used to explore how their accumulation affects cerebral blood vessels, including vascular dysfunction, impaired blood-flow regulation, and mechanisms underlying cerebral amyloid angiopathy (CAA), which is closely linked to Alzheimer’s.
- Neuroinflammation research: Support studies on microglial activation, cytokine release, and inflammatory responses triggered by aggregated beta amyloid species in the Alzheimer’s brain.
- Biomarker and diagnostic studies: Some variants contribute to developing CSF and blood biomarkers (e.g., Aβ (1-42)/Aβ (1-40) ratio) that correlate with amyloid PET imaging and support early Alzheimer’s diagnosis.
- Drug discovery and therapeutic development: Utilized to screen aggregation inhibitors, test monoclonal antibodies, evaluate peptide-based therapeutics, and model strategies that reduce beta-amyloid toxicity or promote clearance in Alzheimer’s research.
- Systemic disease studies: Employed in research examining associations between circulating amyloid-β levels and systemic disorders such as cardiovascular and kidney disease.
- Physiological function studies: Used to investigate potential normal roles of low-level beta amyloid in synaptic regulation, neuronal development, and antioxidant activity.
- Isoform comparison studies: Enables comparison of peptide beta amyloid isoforms (e.g., Aβ (1-40) vs Aβ (1-42)) to assess differences in aggregation behavior, toxicity, and diagnostic relevance in Alzheimer’s research.
Why choose our Amyloid Beta Peptides for your research?
Our Amyloid Beta Peptides are synthesized with high precision to ensure they meet the stringent standards required for neurological and biochemical research. Whether you are investigating plaque formation, prion-like behavior of oligomers, or potential therapeutic interventions, our products offer the purity and consistency necessary for accurate results.
Product Highlights:
- Available in multiple lengths, including full-length Amyloid Beta (1-42) and shorter forms.
- Ideal for Alzheimer's disease research, toxicity assays, and protein misfolding studies.
- Rigorous quality control for reliable aggregation behavior and misfolding characteristics.
Additional product information
Amyloid beta peptide function in Alzheimer’s Disease
- Amyloid beta peptide isoforms are produced from the amyloid precursor protein (APP), a transmembrane protein in neuronal cell membranes known to participate in neuronal growth, synapse formation, and cell signaling.
- Under normal conditions, APP is processed by α- and γ-secretases, generating soluble and non-toxic fragments that are also presumed to support healthy neuronal function.
- When APP is instead cleaved by β- and γ-secretases, insoluble Aβ peptides are formed, which are more prone to misfolding and aggregation. These are proposed to contribute to synaptic regulation, antimicrobial defense, and iron/cholesterol transport.
- Under normal conditions, amyloid-β monomers are typically degraded by enzymes like neprilysin. However, increased production or reduced clearance, for example with age, can lead to their accumulation in the brain.
- The accumulated peptides can then aggregate into β-sheet-rich oligomers and fibrils, which represent early pathological forms.
- These misfolded aggregates can also induce neighboring molecules to misfold, promoting a prion-like chain reaction that accelerates the spread of beta-amyloid pathology.
- As aggregates build up in the extracellular space of neurons, they form insoluble amyloid plaques, which is a defining hallmark of Alzheimer’s disease.
- These plaques can disrupt synaptic communication, trigger oxidative stress, and activate neuroinflammatory responses, ultimately contributing to neuronal dysfunction and cell death.
Amyloid beta peptide structure
- Amyloid-beta monomers are intrinsically disordered, highly soluble, and structurally flexible.
- Their sequence contains hydrophilic and hydrophobic regions, allowing interactions with both aqueous environments and membrane-like surfaces.
- Depending on conditions, monomers may adopt short α-helical segments typical of the soluble state or a more compact conformation around the central hydrophobic region.
- Structural flexibility can expose hydrophobic segments, making the monomers energetically unstable. This drives the monomeric peptides to associate and aggregate with each other to shield these regions.
- As aggregation begins, monomers shift into β-sheet-rich structures forming early oligomers such as parallel or antiparallel dimers. This conformation lets them pack into stable, low-energy assemblies.
- Since peptides with more hydrophobic surface are less stable on their own, they tend to form oligomers faster.
- Aggregation is promoted by conditions that destabilize monomers, including high concentration, acidic pH, hydrophilic-hydrophobic interfaces, or membrane contact.
- These environments favor β-hairpin-like conformations and strengthen intermolecular contacts, producing neurotoxic amyloid beta oligomers.
- With continued growth, oligomers elongate into protofibrils and ultimately form insoluble fibrils characteristic of amyloid plaques.
- These fibrils display the hallmark cross-β-sheet architecture, with strands stacked into highly ordered, stable assemblies.
- They typically consist of intertwined protofilaments with a compact hydrophobic core centered on C-terminal residues, while the N-termini remains flexible.
- The fibrils can have several stable polymorphic structures, depending on environment and peptide length.
Optimized peptides for cutting-edge research
In Alzheimer's research, using the right tools can make all the difference. JPT’s peptides are manufactured to the highest standards to support groundbreaking research and therapeutic discovery. Contact JPT Peptide Technologies GmbH today and our specialized support team will provide you with any information or help you need.