β-Amyloid 1-20

β-Amyloid (1-20) consists of amino acids 1 to 20 of beta amyloid protein.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R1773

CAS No:186319-68-6

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M.F/Formula
C₁₁₃H₁₅₇N₃₁O₃₂
M.W/Mr.
2461.70
Sequence
One Letter Code: DAEFRHDSGYEVHHQKLVFF
three Letter Code: Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe

β-Amyloid 1-20 is a synthetic peptide fragment corresponding to the first 20 amino acids of the amyloid beta (Aβ) protein, a sequence highly relevant to neurodegenerative disease research and protein aggregation studies. As a truncated variant of the full-length amyloid beta peptide, β-Amyloid 1-20 provides a focused model for investigating the molecular determinants of amyloidogenesis, peptide-membrane interactions, and early-stage aggregation phenomena. Its defined sequence and physicochemical properties make it a valuable tool for researchers exploring the mechanistic aspects of peptide folding, oligomerization, and the pathological processes associated with amyloidogenic peptides.

Aggregation studies: β-Amyloid 1-20 is widely utilized in in vitro experiments to elucidate the aggregation propensity of Aβ fragments and to dissect the sequence determinants that drive amyloid fibril formation. Researchers employ this peptide to monitor the kinetics of aggregation, analyze the morphology of resultant aggregates using biophysical techniques such as atomic force microscopy and Thioflavin T fluorescence, and compare the aggregation behavior of truncated peptides to that of longer Aβ variants. These studies enhance understanding of the molecular events leading to amyloid plaque development and provide a foundation for investigating sequence-specific aggregation mechanisms.

Neurotoxicity modeling: In cellular models, β-Amyloid 1-20 serves as a tool for probing the cytotoxic effects of amyloidogenic peptides on neuronal and non-neuronal cells. Its use allows for the systematic evaluation of peptide-induced oxidative stress, membrane disruption, and apoptotic pathways, offering insights into the structure-function relationships that underlie amyloid toxicity. By focusing on this N-terminal fragment, researchers can isolate the contributions of specific sequence motifs to cellular responses and explore the minimal structural requirements for toxicity.

Peptide-membrane interaction studies: The amphipathic nature of β-Amyloid 1-20 makes it an excellent model for investigating peptide interactions with lipid bilayers and artificial membrane systems. Through biophysical assays such as surface plasmon resonance, circular dichroism, and fluorescence spectroscopy, the peptide is employed to characterize binding affinities, conformational changes, and membrane perturbation events. These studies inform the understanding of how amyloid peptides associate with cellular membranes, a process implicated in the disruption of membrane integrity and cellular homeostasis.

Antibody and ligand screening: β-Amyloid 1-20 is frequently used as an antigenic substrate in immunological assays designed to identify and characterize antibodies or small molecules that selectively recognize the N-terminal region of amyloid beta. Its defined sequence facilitates the development and validation of immunoassays, including ELISA and Western blot, for the detection and quantification of Aβ-derived peptides. These applications are crucial for the screening of diagnostic or research reagents targeting amyloidogenic epitopes.

Analytical method development: The peptide is also employed as a standard or reference in the development and optimization of analytical techniques for peptide quantification and characterization. Mass spectrometry, high-performance liquid chromatography, and capillary electrophoresis methods often utilize β-Amyloid 1-20 to calibrate instrumentation, evaluate detection sensitivity, and validate separation protocols. Its defined chemical structure and stability support robust and reproducible analytical workflows, enabling accurate measurement of amyloid peptides in various experimental contexts.

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