DV-40 is a 40-residue peptide comprising hydrophilic, aromatic, and hydrophobic clusters that drive complex folding and aggregation behavior. The sequence allows examination of β-structure formation, membrane interactions, and oligomer kinetics. Researchers use it in high-resolution biophysical assays and structural modeling. Its length supports detailed aggregation-pathway analysis.
CAT No: R2083
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
DV-40 DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV is a synthetic peptide corresponding to a 40-amino acid sequence derived from the amyloid beta (Aβ) protein, specifically the Aβ1-40 fragment. As a well-characterized peptide, it plays a pivotal role in neurodegenerative disease research, particularly in the context of Alzheimer's disease and amyloidogenesis. The sequence is notable for its propensity to aggregate, forming amyloid fibrils that are central to the study of protein misfolding and neurotoxicity. Its defined structure and aggregation behavior make it a critical molecular tool for elucidating the biochemical mechanisms underlying amyloid plaque formation and for exploring the physicochemical properties of amyloidogenic peptides.
Aggregation and Fibrillization Studies: The peptide is extensively utilized to model amyloid fibril formation in vitro, providing a reproducible system for investigating the kinetics and molecular mechanisms of peptide aggregation. Researchers employ it to examine nucleation, elongation, and maturation of amyloid fibrils, enabling the identification of factors that modulate these processes. Such studies are instrumental in understanding the pathogenesis of amyloid-related disorders and in screening for aggregation inhibitors or modulators that may have potential in neurodegenerative disease research.
Structural Biology and Biophysical Characterization: DV-40 enables detailed structural and conformational analyses using a range of biophysical techniques, including nuclear magnetic resonance (NMR), circular dichroism (CD) spectroscopy, and electron microscopy. These approaches facilitate the elucidation of secondary and tertiary structures, oligomerization states, and the impact of environmental variables such as pH, ionic strength, and co-solutes on peptide folding and misfolding. Insights gained from these studies inform the broader understanding of protein aggregation and the molecular determinants of amyloidogenesis.
Cellular Toxicity and Mechanistic Assays: The peptide is frequently incorporated into cellular models to assess the cytotoxic effects of amyloid aggregates on neuronal and non-neuronal cells. By exposing cultured cells to defined concentrations of the peptide in various aggregate states, researchers can quantify cell viability, oxidative stress, and apoptotic responses. These assays are fundamental for dissecting the molecular pathways of amyloid-induced toxicity and for evaluating the protective effects of candidate compounds or genetic modifications.
High-Throughput Screening and Drug Discovery: In the context of therapeutic research, DV-40 serves as a standard substrate in high-throughput screening assays designed to identify small molecules, peptides, or biologics that inhibit or modulate amyloid aggregation. Its reproducible aggregation profile and well-characterized behavior make it an ideal reference compound for validating assay performance and benchmarking the efficacy of novel aggregation modulators. This application is crucial for accelerating the discovery and optimization of research compounds targeting amyloidogenic pathways.
Analytical Method Development and Validation: The peptide is also valuable for developing and validating analytical methods aimed at detecting, quantifying, and characterizing amyloid species. Techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassays rely on synthetic standards like DV-40 to calibrate instruments, standardize protocols, and ensure reproducibility across experiments. These efforts underpin accurate measurement of amyloid content in biological samples and support the advancement of robust analytical workflows in protein aggregation research.
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