cAC 253 is a cyclic peptide derived from a receptor-binding motif that stabilizes β-turn or helical elements. Cyclization constrains backbone mobility, enhancing affinity and selectivity in binding assays. Researchers probe its interaction with neuroendocrine receptors and structural features via NMR or CD. Applications include peptide-hormone analog research, conformational analysis, and ligand-optimization work.
CAT No: R2766
cAC 253 is a synthetic peptide derived from the amyloid precursor protein (APP), specifically corresponding to residues 673-695 of the human sequence. As a well-characterized peptide fragment, it is widely recognized for its relevance in neurodegenerative research, particularly in studies focused on amyloidogenic processing and the molecular mechanisms underlying protein aggregation. Its biochemical properties and sequence specificity make cAC 253 a valuable reagent for probing pathways associated with amyloid formation, cellular signaling, and protein-protein interactions in a variety of experimental systems.
Neuroscience research: cAC 253 is extensively utilized in neuroscience to investigate the processes governing amyloid beta production and deposition. By serving as a defined model peptide, it enables researchers to dissect the enzymatic cleavage events that generate amyloidogenic fragments, providing insights into the early steps of amyloidogenesis. Its sequence homology to regions implicated in neurodegenerative disease pathogenesis allows for the exploration of molecular triggers for aggregation and toxicity in neuronal models.
Protein aggregation studies: The peptide's propensity to form aggregates under specific conditions renders it a useful tool for studying the physicochemical factors influencing amyloid fibril formation. Researchers employ cAC 253 to examine the kinetics and morphology of peptide aggregation, facilitating the identification of modulators and inhibitors that may alter aggregation pathways. These studies contribute to a deeper understanding of the structural determinants of protein misfolding and the development of aggregation-specific probes or assays.
Cell signaling investigations: cAC 253 has been applied to elucidate the impact of amyloidogenic peptides on cellular signaling cascades. By exposing cultured cells or tissue preparations to this peptide, investigators can evaluate alterations in intracellular pathways, receptor activation, and downstream biochemical responses. Such experiments are instrumental in clarifying the molecular links between peptide accumulation and cellular dysfunction, supporting the identification of novel signaling nodes affected by amyloidogenic stress.
Analytical method development: The defined sequence and physicochemical properties of cAC 253 make it an ideal standard or reference material in analytical workflows. It is frequently used in the calibration and validation of mass spectrometry, chromatography, and immunoassay techniques designed to detect and quantify amyloid-related peptides. Its inclusion in assay development ensures reliable performance and enhances the accuracy of peptide detection in complex biological samples.
Peptide-protein interaction analysis: cAC 253 serves as a model ligand in studies aiming to map binding sites and characterize the affinity of interactions between amyloidogenic peptides and their protein partners. Through techniques such as surface plasmon resonance, isothermal titration calorimetry, or co-immunoprecipitation, researchers can delineate the molecular basis of peptide-mediated interactions, advancing the understanding of protein network perturbations associated with amyloid formation. These applications support the rational design of molecules that modulate or disrupt pathogenic peptide-protein associations in fundamental research contexts.
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