β-amyloid (15-21) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.
β-Amyloid 15-21 is a synthetic peptide fragment derived from the central hydrophobic core region of the amyloid beta (Aβ) protein. As a defined segment corresponding to residues 15 through 21 of the full-length Aβ sequence, it is highly valued in neurobiological research for its relevance to amyloid aggregation, protein-protein interaction studies, and the mechanistic investigation of neurodegenerative processes. The peptide's sequence, central to the aggregation-prone domain of Aβ, renders it an essential tool for dissecting the molecular underpinnings of amyloid formation and its associated pathologies. Its physicochemical properties make it a versatile probe for structural, biochemical, and biophysical applications in the context of protein misfolding and aggregation.
Aggregation studies: The peptide is widely utilized to model and analyze the early stages of amyloid fibril formation in vitro. Its sequence, representing a critical hydrophobic stretch of the amyloid beta protein, allows researchers to investigate the nucleation and elongation phases of peptide self-assembly. By employing β-Amyloid 15-21 in aggregation assays, scientists can elucidate the sequence determinants and environmental factors that modulate amyloidogenic propensity, providing valuable insights into the molecular mechanisms underlying protein misfolding disorders.
Protein-protein interaction analysis: As a representative core motif of the full-length Aβ protein, this peptide serves as a molecular probe for mapping interaction sites with other biomolecules, including chaperones, antibodies, and small-molecule inhibitors. Its defined sequence enables detailed studies on binding specificity, affinity, and structural compatibility, facilitating the identification of interaction partners that may modulate amyloid formation or stability. Such research supports the rational design of molecular tools and potential modulators targeting amyloidogenic regions.
Structural biology research: The defined length and sequence of β-Amyloid 15-21 make it suitable for high-resolution structural investigations using techniques such as NMR spectroscopy, X-ray crystallography, and cryo-electron microscopy. Researchers employ this peptide to characterize secondary structure propensities, intermolecular interactions, and conformational dynamics in solution or bound states. These structural insights are critical for understanding the physicochemical basis of amyloid fibril formation and for guiding the development of structure-based modulators.
Peptide-based inhibitor screening: The fragment is employed as a model substrate in screening assays designed to identify and characterize compounds that interfere with amyloid self-assembly. By monitoring the aggregation behavior of β-Amyloid 15-21 in the presence of candidate inhibitors, researchers can rapidly assess the efficacy and mechanism of action of small molecules, peptides, or antibodies. This approach accelerates the discovery and optimization of agents aimed at modulating amyloidogenic pathways in vitro.
Analytical method development: Owing to its well-defined sequence and aggregation properties, the peptide is frequently used as a standard or reference material in the development and validation of analytical techniques for amyloid detection and quantification. Applications include calibration of mass spectrometry protocols, optimization of chromatographic separation methods, and benchmarking of fluorescence- or dye-based aggregation assays. Such uses support the advancement of robust and reproducible tools for amyloid research and diagnostics in laboratory settings.
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