Aβ1-14-εK-KKK-MvF5 Th integrates an Aβ(1-14) fragment with additional lysine-rich extensions and an MvF5 tag for tracking aggregation behavior. Researchers use it to monitor early oligomer formation, peptide-membrane interactions, and sequence-driven fibrillization. The construct provides strong spectroscopic handles for real-time assays. Applications include amyloid-mechanism research and aggregation-modulator screening.
CAT No: Z10-101-227
Aβ1-14-εK-KKK-MvF5 Th is a synthetic carbohydrate-peptide conjugate designed for advanced research applications in the fields of neuroscience, immunology, and molecular biology. Featuring a unique sequence derived from the amyloid beta (Aβ) peptide and incorporating a specialized ε-lysine (εK) linker with a multivalent KKK motif, this compound is coupled with the MvF5 Th moiety to enhance its biochemical versatility. The structural configuration of Aβ1-14-εK-KKK-MvF5 Th enables precise molecular interactions and facilitates its integration into complex experimental systems. Its water solubility and stability under physiological conditions make it a valuable tool for studies requiring consistent and reproducible results. Researchers benefit from its well-defined composition, which allows for accurate interpretation of experimental outcomes and the development of innovative methodologies in carbohydrate and peptide research.
Neurodegenerative Disease Modeling: Aβ1-14-εK-KKK-MvF5 Th is extensively utilized in the modeling of neurodegenerative diseases, particularly those involving amyloid beta aggregation and plaque formation. By mimicking key epitopes of the native Aβ sequence, this conjugate serves as a critical probe for investigating the early events of amyloidogenesis and the molecular mechanisms underlying neurotoxicity. Its unique structure enables the assessment of aggregation kinetics, the screening of aggregation inhibitors, and the evaluation of novel therapeutic strategies in vitro. The inclusion of the multivalent KKK motif enhances its capacity to form defined oligomeric species, thereby providing a robust platform for dissecting the pathological processes associated with amyloid accumulation and neuronal dysfunction.
Immunological Assays and Antibody Development: The conjugation of the Aβ1-14 sequence with MvF5 Th creates a potent antigenic substrate for immunological assays and antibody generation. Researchers employ this compound in ELISA, Western blotting, and immunoprecipitation experiments to detect and quantify specific antibodies against amyloid beta epitopes. Its defined structure and enhanced immunogenicity facilitate the evaluation of immune responses in experimental models, supporting the development of monoclonal and polyclonal antibodies with high specificity. Additionally, the εK-KKK linker provides spatial orientation that preserves epitope accessibility, improving assay sensitivity and reproducibility in antibody screening platforms.
Protein-Protein Interaction Studies: The modular design of Aβ1-14-εK-KKK-MvF5 Th makes it a valuable tool for investigating protein-protein interactions relevant to amyloid biology. By serving as a bait molecule in pull-down assays or surface plasmon resonance experiments, it enables the identification and characterization of binding partners involved in amyloid processing and clearance. The presence of the multivalent KKK motif enhances the avidity of interactions, allowing for the detection of low-affinity binding events that might be missed with shorter or less complex peptides. This application is particularly significant for elucidating the roles of chaperones, receptors, and degradation enzymes in the regulation of amyloid homeostasis.
Glycobiology and Carbohydrate Recognition: The carbohydrate component of Aβ1-14-εK-KKK-MvF5 Th provides a strategic advantage for studies focused on carbohydrate-protein interactions and glycan recognition. Researchers utilize it to probe the binding specificity of lectins, glycosidases, and carbohydrate-binding modules in various assay formats. Its defined glycan structure supports the systematic analysis of glycan-mediated cellular processes, including cell signaling, adhesion, and immune modulation. The compound's stability and solubility further facilitate high-throughput screening and quantitative binding studies, advancing the understanding of glycan function in health and disease.
Peptide-Based Diagnostic Tool Development: Leveraging its unique hybrid structure, Aβ1-14-εK-KKK-MvF5 Th is employed in the development of peptide-based diagnostic tools for research applications. Its ability to mimic disease-relevant epitopes and engage in specific molecular interactions underpins its utility in biosensor design and biomarker discovery. By incorporating this molecule into diagnostic platforms, researchers can achieve sensitive and selective detection of amyloid beta-related biomarkers in complex biological samples. The versatility of its peptide-carbohydrate conjugate format allows for customization and integration into a variety of assay systems, supporting the advancement of innovative diagnostic technologies.
Chemical Biology and Structure-Activity Relationship Studies: In chemical biology, Aβ1-14-εK-KKK-MvF5 Th serves as a model compound for dissecting structure-activity relationships in peptide and carbohydrate conjugates. Researchers synthesize analogs and derivatives to systematically explore how modifications in peptide sequence, glycan composition, or linker architecture influence biological activity and molecular recognition. Such studies inform the rational design of new research tools and therapeutic candidates, expanding the scope of carbohydrate-peptide chemistry. The detailed characterization of Aβ1-14-εK-KKK-MvF5 Th's interactions and functional properties provides a foundation for advancing both fundamental and applied research in molecular biosciences.
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