β-Amyloid (1-28) is a β-Amyloid protein fragment involved in metal binding. Beta-amyloid is a peptide that forms amyloid plaques in the brains of Alzheimer's disease (AD) patients.
CAT No: R1776
CAS No:109770-29-8
Synonyms/Alias:109770-29-8;Amyloid beta-Protein (1-28);BETA-AMYLOID (1-28);PAB-4481-V;Amyloid ?-Protein (Human, 1-28);Amyloid beta-Protein (1-28) trifluoroacetate salt;SP-28 (Human);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;
β-Amyloid 1-28 is a synthetic peptide corresponding to the first 28 amino acids of the amyloid beta (Aβ) protein, a key fragment implicated in neurodegenerative research, particularly studies involving Alzheimer's disease pathology. As a well-defined peptide sequence, it serves as a valuable tool for investigating the molecular underpinnings of amyloid aggregation, protein-protein interactions, and the cellular processes associated with amyloidogenic pathways. Researchers utilize this fragment to dissect the structural and functional aspects of amyloid peptides, enabling precise exploration of mechanisms that govern peptide misfolding and neurotoxicity. Its defined length and biochemical properties make it especially suitable for in vitro studies where controlled experimental conditions are essential for elucidating the complex behavior of amyloidogenic peptides.
Aggregation studies: β-Amyloid 1-28 is widely used in aggregation assays to model the initial stages of amyloid fibril formation. Its truncated sequence provides insight into the minimal structural requirements for self-assembly, allowing researchers to monitor aggregation kinetics, identify nucleation events, and characterize oligomerization pathways. By employing this peptide in biophysical and spectroscopic analyses, scientists gain a deeper understanding of the conformational transitions that drive amyloid plaque development, which is central to neurodegenerative disease research.
Neurotoxicity modeling: In cellular assays, the 1-28 fragment is applied to examine the cytotoxic effects of amyloid peptides on neuronal and glial cells. Its use enables the assessment of peptide-induced oxidative stress, membrane disruption, and apoptotic signaling within a controlled experimental framework. By comparing the biological activity of this fragment to longer or full-length amyloid beta peptides, investigators can delineate the sequence determinants responsible for neurotoxicity, thus advancing the identification of critical domains involved in disease-relevant cellular responses.
Antibody validation: The defined epitope sequence of β-Amyloid 1-28 makes it an essential reagent for validating the specificity and sensitivity of anti-amyloid antibodies. Researchers employ the peptide in immunoassays, such as ELISA and western blotting, to confirm antibody binding to the N-terminal region of amyloid beta. This application is crucial for the development and quality control of immunodetection tools used in both basic research and preclinical studies, ensuring reliable detection of amyloid species in complex biological samples.
Peptide interaction studies: The 1-28 fragment is instrumental in mapping protein-peptide and peptide-peptide interactions relevant to amyloidogenic processes. By using this sequence in binding assays and structural studies, scientists can identify molecular partners that modulate aggregation or clearance of amyloid peptides. Such investigations contribute to the broader understanding of cellular mechanisms that regulate amyloid homeostasis, offering potential targets for modulating peptide behavior in vitro.
Structural analysis: Due to its manageable length and well-characterized sequence, β-Amyloid 1-28 is frequently utilized in high-resolution structural studies, including nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography. These approaches facilitate detailed examination of secondary structure formation, conformational dynamics, and the influence of environmental factors on peptide folding. Structural insights gained from such studies are foundational for rational design of inhibitors or modulators targeting amyloid aggregation, supporting the advancement of molecular research in neurodegenerative disorders.
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