β-Amyloid (1-40) is a primary protein in plaques found in the brains of patients with Alzheimer's disease.
CAT No: R1778
CAS No:131438-79-4
Synonyms/Alias:beta-Amyloid 1-40;131438-79-4;Abeta40;Human beta-amyloid peptide (1-40);Abeta40 [MI];Abeta(1-40);beta-Amyloid protein(1-40);UNII-13539D6GO8;Human beta-amyloid peptide-(1-40);Amyloid beta peptide(1-40) (synthetic);13539D6GO8;Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val;beta-Amyloid (1-40);Beta-Amyloid(1-40);beta-amyloid 40;DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV;Beta-amyloid protein 40;CHEBI:64646;Amyloid beta-Peptide 1-40 TFA;EX-A7736;AKOS024456454;FA110057;(Asn7)-Amyloid b-Protein (1-40) trifluoroacetate salt;H-Asp-Ala-Glu-Phe-Arg-His-Asn-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe- Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-G ly-Leu-Met-Val-Gly-Gly-Val-Val-OH; H-DAEFRHNSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV-OH;
β-Amyloid 1-40 is a synthetic peptide corresponding to the first 40 amino acids of the human β-amyloid protein, a key fragment derived from the amyloid precursor protein (APP) through sequential proteolytic processing. This peptide is widely recognized for its central role in neurodegenerative research, particularly in the study of amyloid plaque formation and the molecular mechanisms underlying Alzheimer's disease. Its defined sequence and aggregation properties make it a valuable biochemical tool for elucidating the structural and functional aspects of amyloidogenesis, protein misfolding, and peptide aggregation phenomena. As a research-grade peptide, β-Amyloid 1-40 is indispensable for laboratories investigating the biophysical, cellular, and molecular events associated with amyloid pathology and related neurobiological processes.
Aggregation studies: β-Amyloid 1-40 is extensively used in aggregation assays to investigate the kinetics and thermodynamics of amyloid fibril formation. Researchers employ this peptide to model the nucleation and elongation phases of amyloid aggregation in vitro, enabling the characterization of fibrillar and oligomeric intermediates. These studies provide foundational insights into the physicochemical factors that drive peptide self-assembly, including solvent conditions, concentration effects, and sequence-specific interactions, which are critical for understanding the molecular basis of amyloid-related disorders.
Neurotoxicity research: The peptide serves as a model agent for probing the cytotoxic effects of amyloid aggregates on neuronal and glial cells. By exposing cultured neural cells to β-amyloid 1-40, investigators can assess cellular responses such as oxidative stress, apoptosis, and synaptic dysfunction. These experiments help delineate the pathways by which amyloid species compromise cell viability and contribute to neurodegeneration, offering a platform for the identification and evaluation of protective strategies or modulators of toxicity.
Screening of aggregation inhibitors: The defined aggregation behavior of β-amyloid 1-40 makes it an ideal substrate for high-throughput screening of small molecules, peptides, or antibodies that modulate amyloid formation. Researchers utilize this peptide in biochemical and biophysical assays to quantify the efficacy of candidate inhibitors in preventing fibril growth or destabilizing existing aggregates. These screening campaigns are pivotal for the discovery and mechanistic validation of compounds with potential to mitigate amyloid pathology at the molecular level.
Structural biology investigations: β-Amyloid 1-40 is frequently employed in advanced structural studies, including nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), and cryo-electron microscopy (cryo-EM). By analyzing the conformational transitions and secondary structure elements of this peptide under various experimental conditions, scientists gain detailed knowledge of the molecular architecture of amyloid fibrils and oligomers. Such insights are essential for the rational design of structure-based probes and inhibitors targeting amyloidogenic peptides.
Development of detection assays: The peptide is also utilized as a standard or calibrator in the development and validation of analytical assays for amyloid quantification, such as enzyme-linked immunosorbent assays (ELISA), fluorescence-based detection, and mass spectrometry protocols. Incorporating β-amyloid 1-40 into assay development ensures specificity and sensitivity in the measurement of amyloid species in complex biological samples, supporting biomarker discovery and the refinement of diagnostic methodologies for neurodegenerative research.
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