β-Amyloid (1-16) 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: R1771
CAS No:131580-10-4
Synonyms/Alias:131580-10-4;Amyloid beta-Protein (1-16);beta-Amyloid (1-16);Amyloid beta-Protein (1-16) trifluoroacetate salt;DA-50447;
β-Amyloid 1-16 is a synthetic peptide fragment corresponding to the N-terminal residues 1 through 16 of the amyloid beta (Aβ) protein, a key molecular species implicated in neurodegenerative research. As a well-characterized segment of the larger amyloid beta peptide, it offers unique advantages for dissecting the structural and functional properties of amyloidogenic sequences. Its defined length and sequence specificity make it highly relevant for studies investigating the early events of amyloid aggregation, protein-protein interactions, and the molecular mechanisms underlying neurobiological processes. Researchers utilize this peptide as a model system to elucidate the role of N-terminal regions in Aβ biology, providing foundational insights into protein misfolding, aggregation pathways, and related pathologies.
Aggregation studies: β-Amyloid 1-16 serves as a valuable substrate for examining the initial stages of amyloid formation, particularly the nucleation and oligomerization processes that precede fibril assembly. Its truncated sequence allows researchers to isolate the contributions of the N-terminal domain to aggregation kinetics and morphology, enabling detailed investigations into the molecular determinants that govern amyloidogenicity. By comparing the behavior of this fragment with longer Aβ peptides, scientists can delineate sequence-dependent factors that influence aggregation propensity and structural transitions.
Protein interaction analysis: The peptide is frequently employed in binding assays to probe interactions with metal ions, antibodies, or small-molecule modulators. Its N-terminal residues are known to participate in metal coordination and epitope recognition, making it an ideal tool for characterizing binding affinities, mapping interaction sites, and screening for compounds that modulate Aβ-related pathways. Such studies are critical for understanding the molecular specificity of ligand recognition and for advancing the rational design of aggregation inhibitors or diagnostic reagents.
Structural biology research: β-Amyloid 1-16 is instrumental in high-resolution structural studies, including nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography, aimed at elucidating the conformational properties of amyloidogenic segments. Its manageable size and solubility facilitate detailed analysis of secondary structure, backbone dynamics, and solvent interactions. Insights gained from these structural investigations inform broader models of amyloid assembly and provide reference data for computational simulations of peptide folding and misfolding.
Antibody development: The defined sequence of this peptide fragment is widely utilized as an immunogen or screening target in the generation and characterization of Aβ-specific antibodies. Researchers employ it in enzyme-linked immunosorbent assays (ELISA), western blotting, and immunohistochemistry to assess antibody specificity, affinity, and cross-reactivity. This application is essential for developing reliable research tools, validating antibody performance, and supporting the discovery of novel detection reagents for amyloid-related studies.
Analytical method calibration: β-Amyloid 1-16 is also used as a standard or reference material in mass spectrometry, chromatography, and other quantitative analytical techniques. Its well-defined physicochemical properties allow accurate calibration of instrumentation, validation of peptide quantification protocols, and benchmarking of analytical workflows. This role is particularly important for ensuring reproducibility, sensitivity, and accuracy in the detection and measurement of amyloidogenic peptides in complex biological samples.
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