S26C-Beta-Amyloid (1-40) Dimer HFIP treated

S26C-Beta-Amyloid (1-40) Dimer (HFIP treated) is a chemically stabilized, covalently linked dimer of the human Beta-amyloid (1-40) peptide. It is created by introducing a Cysteine substitution at position 26, which enables stable disulfide-bond formation between two monomers. This construct mimics early toxic Beta-amyloid (1-40) oligomers and offers higher stability and reproducibility than spontaneously formed assemblies. It is widely used in Alzheimer’s research to study aggregation, oligomerization, and early pathogenic mechanisms.

HFIP treatment removes higher-order aggregates before use, providing a clean and consistent dimeric starting state for aggregation assays. For research use only!

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.

S26C-Beta-Amyloid (1-40) Dimer HFIP treated - Specifications

• Purity: >95% (HPLC-MS)
• Delivery Format: Freeze-dried in plastic vial
• CAS: 1802087-75-7
• Application(s):
• Condition(s)/Topic(s): Alzheimer's disease
• Standard Delivery Time: 2-5 days

Are you interested in other Amyloid Beta A4 Peptides? We also offer unmodified Beta-Amyloid (1-40)!

You can also choose your amyloid beta sequence, amount and purity. We will assist you along the way! Custom Peptide Synthesis.

Research areas and applications:

• Alzheimer’s and neurodegenerative research: Used as a defined model of early Beta-amyloid (1-40) oligomers to study initial pathogenic events in Alzheimer’s disease and related neurodegenerative conditions.
• Amyloid aggregation and plaque formation studies: Provides a controlled starting point for tracking the conversion of dimers into higher-order oligomers and protofibrils using structural techniques such as NMR, AFM, and TEM.
• Early neurotoxicity and synaptic dysfunction studies: Enables analysis of how stabilized amyloid beta dimers disrupt synaptic signaling, impair membranes, induce oxidative stress, and contribute to neuronal dysfunction.
• Memory and LTP impairment studies: Applied in neuronal and animal models to investigate how amyloid beta dimers impair long-term potentiation and drive early cognitive decline.
• Seeding and propagation research: Used to examine how defined amyloid beta dimers act as seeds that accelerate aggregation or influence amyloid propagation behavior.
• Protein-peptide, receptor, and membrane interactions: Applied to study how early the 40-amino-acid long amyloid beta oligomers bind to lipid bilayers, neuronal receptors (e.g., PrP), and other membrane components involved in amyloid beta toxicity.
• Anti-amyloid drug discovery and therapeutic development: Utilized for screening aggregation inhibitors, testing monoclonal antibodies, and evaluating small molecules targeting early oligomer formation or toxicity.
• Structure-function analyses: Supports detailed studies of dimer structure, stability, and conformational changes, linking specific structural features to downstream toxicity.
• Comparative studies: Enables direct comparison with monomeric amyloid beta peptides to assess differences in aggregation, toxicity, and oligomer behavior.

Benefits

• Defined dimeric species: Provides a covalently linked, structurally uniform and stable S26C-Beta-Amyloid (1-40) dimer for experiments.
• High reproducibility: Eliminates batch-to-batch variability by avoiding heterogeneous or spontaneously formed oligomer mixtures.
• Clean and reliable starting material: HFIP treatment removes higher-order aggregates, ensuring a well-prepared and consistent dimeric state.
• Enhanced experimental control: The engineered disulfide bond preserves the stable dimeric form, enabling precise initiation and monitoring of aggregation, toxicity, and structural assays.

Key concepts

What is a HFIP treatment?

Hexafluoroisopropanol (HFIP) is a highly fluorinated solvent that disrupts hydrogen bonding and dissolves peptide aggregates. For the S26C-Beta-Amyloid (1-40) Dimer, HFIP removes non-covalent higher-order assemblies around the disulfide-linked dimer by destabilizing β-sheet interactions. This treatment keeps the covalent dimer intact while providing a clean, well-defined, and reproducible dimeric starting material for controlled experiments.

JPT's Single Catalog Peptides
S26C-Beta-Amyloid (1-40) Dimer (HFIP treated) 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