β-Amyloid (25-35) (Amyloid beta-peptide (25-35)) is the fragment Aβ(25-35) of the Alzheimer's amyloid β-peptide, has shown neurotoxic activities in cultured cells.
CAT No: HB00080
CAS No:131602-53-4
Synonyms/Alias:131602-53-4;AMYLOID BETA-PROTEIN (HUMAN, 25-35) TRIFLUOROACETATE;DTXSID80392197;Amyloid beta-peptide(25-35);2-[[2-[[2-[[2-[[2-[2-[[2-[[6-amino-2-[[4-amino-2-[[2-[(2-aminoacetyl)amino]-3-hydroxypropanoyl]amino]-4-oxobutanoyl]amino]hexanoyl]amino]acetyl]amino]propanoylamino]-3-methylpentanoyl]amino]-3-methylpentanoyl]amino]acetyl]amino]-4-methylpentanoyl]amino]-4-methylsulfanylbutanoic acid;Amyloid beta-Protein(25-35);glycylserylasparaginyllysylglycylalanylisoleucylisoleucylglycylleucylmethionine;Amyloid -Protein (25-35);Abeta25-35;Amyloid beta-Protein (25-35) trifluoroacetate salt;beta-Amyloid (25-35)?;DTXCID30343058;AS-76186;DA-61040;Amyloid |A-Protein(25-35);Amyloid -Protein (25-35);AMYLOIDBETA-PROTEIN(HUMAN,25-35)TRIFLUOROACETATE;Amyloid beta-Protein(25-35);Amyloid -Protein (25-35);
Amyloid β-Protein(25-35) is a synthetic peptide fragment derived from the C-terminal region of the amyloid beta (Aβ) protein, a molecule extensively studied for its role in neurodegenerative processes, particularly those associated with Alzheimer's disease pathology. As the shortest sequence of Aβ capable of forming amyloid fibrils and exhibiting neurotoxic properties in vitro, this peptide serves as a valuable model for exploring the biophysical and biochemical mechanisms underlying amyloid aggregation and cytotoxicity. Its solubility, aggregation propensity, and ability to induce cellular responses make it a widely utilized tool in neurobiology, molecular pharmacology, and peptide research.
Neurotoxicity modeling: Researchers frequently employ the 25-35 fragment to replicate amyloid-induced cytotoxicity in neuronal and glial cell cultures. Due to its robust ability to aggregate and elicit oxidative stress, mitochondrial dysfunction, and apoptotic signaling, this peptide provides a reliable platform for studying the cellular events triggered by amyloid accumulation. Such models are instrumental in dissecting the mechanisms of neuronal injury, synaptic dysfunction, and glial activation, thereby advancing the understanding of neurodegenerative disease processes.
Protein aggregation studies: The fragment's pronounced tendency to self-assemble into β-sheet-rich fibrils makes it an ideal substrate for investigating the molecular dynamics of amyloid formation. Scientists utilize it to examine nucleation, elongation, and maturation of amyloid fibrils using techniques such as fluorescence spectroscopy, electron microscopy, and X-ray diffraction. These studies elucidate the physicochemical principles governing peptide aggregation and contribute to the broader field of protein misfolding disorders.
Screening of aggregation inhibitors: The reproducible aggregation behavior of this peptide fragment facilitates high-throughput screening of small molecules, peptides, or natural products that can modulate amyloid formation. By serving as a target in inhibitor assays, it enables the identification and characterization of compounds with potential to disrupt or prevent pathological aggregation. Such screening is critical for early-stage drug discovery efforts focused on neurodegenerative disease intervention at the molecular level.
Oxidative stress and cellular signaling research: The 25-35 sequence is often utilized to induce oxidative stress in neuronal models, providing a controlled means of studying redox biology and cellular defense mechanisms. Its capacity to provoke reactive oxygen species generation and alter intracellular signaling pathways allows for detailed examination of antioxidant responses, mitochondrial integrity, and the interplay between oxidative damage and cell fate decisions. These insights are essential for unraveling the complex cascade of events implicated in neuronal degeneration.
Peptide structure-function analysis: As a minimal yet bioactive region of the amyloid beta protein, this fragment is a valuable reference for structure-activity relationship studies. Researchers employ it to probe the influence of sequence modifications, post-translational mimetics, or chemical modifications on aggregation kinetics and biological activity. Such analyses inform the rational design of peptide analogs, the development of aggregation probes, and the elucidation of key structural determinants driving amyloidogenicity and toxicity.
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