Beta-Amyloid (1-42) HFIP treated

Beta-amyloid (1-42), also known as Aβ (1-42), is a 42-amino acid peptide generated from the human amyloid precursor protein (APP) and is thought to contribute to neuronal function. When its clearance is impaired, the peptide rapidly aggregates into β-sheet-rich oligomers and fibrils that initiate amyloid plaque formation and promote neuronal damage. Known as the more aggregation-prone isoform, this peptide is strongly linked to Alzheimer’s disease and widely used in neurodegenerative research to study rapid aggregation events, neurotoxicity, and early plaque formation.

HFIP treatment breaks down pre-formed aggregates and returns Amyloid beta 1 42 peptides to a monomeric state, ensuring a reproducible and clean starting material for experiments. For research use only, do not use in humans!

Produced by JPT Peptide Technologies, a leader in custom peptide synthesis for Alzheimer’s research.

Synthetic peptide derived from the N-terminal region of human Amyloid beta A4 protein (Swiss-Prot ID: P05067). HFIP treatment is performed to disrupt beta-sheets and other unwanted secondary structures.

Beta-Amyloid (1-42) HFIP treated - Specifications

• Purity: >95% (HPLC-MS)
• Delivery Format: Freeze-dried in plastic vial
• CAS: 107761-42-2
• Application(s):
• Condition(s)/Topic(s): Alzheimer's disease
• Standard Delivery Time: 2-5 days

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Role of Beta amyloid (1-42) in Alzheimer’s disease?

1. In the human brain, Beta amyloid (1-42) is produced through proteolytic processing of the amyloid precursor protein (APP), a large transmembrane protein located in neuronal membranes. Although its complete physiological function remains unclear, APP is presumed to be involved in neuronal growth, synapse formation, cell adhesion and intracellular communication.
2. Under normal physiological conditions, APP is cleaved by α- and γ-secretases, generating soluble and non-toxic peptide fragments that also contribute to regulatory processes in neurons.
3. However, when processed by β- and γ-secretases, APP produces insoluble amyloid beta peptides such as Aβ (1-40) and Aβ (1-42). These peptides are suggested to be involved in synaptic activity, antimicrobial defense and iron/cholesterol transport.
4. Among these peptides, the 42-amino-acid variant is the more aggregation-prone isoform due to its additional hydrophobic C-terminal residues. When production increases or clearance is reduced with age, Amyloid β (1-42) monomers readily aggregate on their own, or sometimes together with Amyloid β (1-40), into β-sheet-rich oligomers and fibrils.
5. These aggregated species accumulate in the extracellular space of neurons and initiate the formation of insoluble amyloid plaques, which is one of the pathological hallmarks of Alzheimer’s disease. Because this isoform aggregates more rapidly and forms more stable oligomers than beta amyloid 1-40, it dominates the early stages of plaque development.
6. The buildup of amyloid beta aggregates can then disrupt synaptic communication and trigger neuroinflammatory responses, which over time contribute to neuronal dysfunction and cell death. Amyloid-β (1-42)-rich deposits are well recognized for their high neurotoxic potential.

Through these mechanisms, Beta amyloid 1-42 peptide plays a central role in the pathogenesis of Alzheimer’s disease and related neurodegenerative disorders, a role that is still being further clarified.

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Structure of Beta Amyloid (1-42), CAS: 107761-42-2

Beta amyloid (1-42) is a 42-amino-acid peptide with a highly dynamic structure that depends strongly on its environment and aggregation state. The peptide can exist in three principal structural forms:

Monomers:

• As a monomer, Abeta (1-42) is intrinsically disordered and adopts flexible conformations. Its mix of hydrophilic and hydrophobic residues allows brief dispersion in solution and supports interactions with membrane-like surfaces. However, its long hydrophobic C-terminal region limits monomer stability and encourages early self-association.
• The monomers can form short α-helical segments near membranes or fold into more compact structures around its central hydrophobic region depending on the environment.

Oligomers:

• As aggregation begins, the monomers rapidly adopt β-sheet-rich structures and assemble into small oligomers, such as parallel and antiparallel dimers. These oligomers are considered highly neurotoxic, as they can disrupt neuronal homeostatis.
• Its extended hydrophobic C-terminal region accelerates oligomerization at hydrophilic-hydrophobic interfaces, where peptides come into close proximity and readily form aggregation-prone, β-hairpin-like conformations.

Fibrils:

• As oligomers grow, Abeta (1-42) forms protofibrils and then insoluble fibrils that contribute to amyloid plaque formation. These fibrils exhibit the typical cross-β-sheet architecture, with strands stacked into highly ordered assemblies.
• They are typically built from intertwined protofilaments containing a compact hydrophobic core enriched in C-terminal residues, while the N-terminus remains flexible. These fibrils can form several stable polymorphic structures.

Research areas and applications

• Neurodegeneration and Alzheimer’s research: Used to study how Amyloid beta 1-42 overproduction, impaired clearance, and rapid aggregation drive Alzheimer’s progression due to its high neurotoxicity and strong synaptic impact.
• Amyloid aggregation and plaque formation studies: Serves as a model for fast β-sheet nucleation, toxic oligomer formation, and the development of protofibrils and mature fibrils using NMR, AFM, and cryo-EM.
• Neurotoxicity, synaptic physiology, and neuronal function: Used to examine how beta amyloid oligomers disrupt synaptic signaling, alter calcium balance, impair plasticity, induce oxidative stress, and activate apoptosis that contributes to neuronal dysfunction.
• Anti-amyloid drug discovery and therapeutic development: Utilized to screen aggregation inhibitors, test Aβ-targeting monoclonal antibodies (e.g., beta amyloid 1-42 antibody), evaluate peptide-based therapeutics, and model compound effects that reduce amyloid burden.
• Biomarker development and diagnostics: Supports CSF and blood biomarker studies focused on decreased peptide levels and its ratio with Amyloid beta (1-40), both strongly linked to amyloid PET imaging and early Alzheimer’s diagnosis.
• APP processing and familial Alzheimer’s disease research: Used to analyze how APP, PSEN1, and PSEN2 mutations shift γ-secretase cleavage toward increased Amyloid beta (1-42), modeling mechanisms of familial Alzheimer’s disease.
• Neuroinflammation research: Applied to study microglial and astrocytic activation, cytokine release, and inflammatory responses induced by Amyloid beta aggregates that stimulate innate immune pathways.
• Seeding and cross-seeding studies: Used to examine how it acts as a nucleation seed for Aβ (1-40) fibrillization and how mixed Aβ species form distinct fibril structures in plaques.
• Comparison studies with Aβ (1-40): Used to compare aggregation kinetics, toxicity, structural stability, and diagnostic relevance with Beta amyloid (1-40).

Benefits and limitations

A brief overview of the peptide’s strengths and limitations in experimental studies is shown below:

Key Concepts

Why do Amyloid beta peptides aggregate?

Amyloid beta peptides aggregate because several regions in their sequence are strongly hydrophobic and energetically unstable when exposed to water. In their flexible and disordered monomeric form, these hydrophobic surfaces can become exposed, prompting the peptides to associate so they can shield them from the surrounding solution.

As they come together, the molecules readily adopt beta sheet structures that allow many peptides to pack into stable and low energy assemblies. Variants with more hydrophobic content, such as the 42-amino-acid isoform, make this transition more easily and therefore show a stronger tendency to aggregate.

Aggregation is further supported by factors such as higher peptide concentration, acidic pH, interactions with membranes, or the presence of metal ions, which destabilize the monomer and promote the formation of oligomers and eventually fibrils.

What is a HFIP treatment?

Hexafluoroisopropanol (HFIP) is a strongly fluorinated solvent widely used in peptide research because it disrupts hydrogen bonds and can solubilize peptide assemblies that are otherwise difficult to dissolve. In studies involving amyloid beta, HFIP is used to break apart existing fibrils and oligomers by interfering with their beta sheet structures. This treatment returns the Abeta peptides to their monomeric forms and ensures a consistent, well defined starting point for controlled experimental work.

JPT's Single Catalog Peptides
Beta Amyloid 1-42 belongs to our Single Catalog Peptides and is manufactured according to the same high-quality standards applied across our peptide catalog. JPT Peptide Technologies has substantial, long-standing expertise in providing peptides, peptidomimetics, and proteins to the global scientific community. Our highly skilled and committed scientific staff ensures that the most appropriate methods and techniques are selected for every synthesis project. All of JPT's catalog peptides are provided with HPLC-MS analyses to confirm the identity and demonstrate the high quality of our peptides.

Benefits of JPT's Single Catalog Peptides
- Synthesis protocols designed to avoid toxic contaminants and side products
- Provision of freeze dried aliquots for enhanced stability
- Proven track record for applications in clinical studies