COG 133 is a fragment of Apolipoprotein E (APOE) peptide. COG 133 competes with the ApoE holoprotein for binding the LDL receptor, with potent anti-inflammatory and neuroprotective effects. COG 133 is also a nAChR antagonist with an IC50 of 445 nM.
apoE(133-149) is a synthetic peptide fragment derived from the apolipoprotein E (apoE) protein, encompassing amino acid residues 133 to 149 of the native sequence. As a well-defined segment of apoE, this peptide is of significant interest in biochemical and molecular research due to its involvement in protein-protein interactions, lipid binding, and receptor recognition processes. The 133-149 region of apoE is recognized as a critical domain influencing the protein's structural conformation and functional activity, making it a valuable tool for investigating the mechanistic aspects of apoE-related pathways. Its defined sequence and physicochemical properties enable precise experimental manipulation in studies exploring the roles of apoE in lipid metabolism, neurobiology, and cellular signaling.
Receptor binding studies: The apoE(133-149) peptide is widely utilized in assays designed to elucidate the molecular interactions between apolipoprotein E and its cellular receptors, such as the low-density lipoprotein receptor (LDLR) family. The 133-149 region contains key residues implicated in receptor recognition and binding affinity, allowing researchers to dissect the structural determinants required for receptor-mediated endocytosis and cellular uptake of lipoprotein particles. By applying this peptide in receptor binding assays, scientists can map critical contact points, analyze binding kinetics, and investigate the influence of specific mutations or modifications within the apoE sequence.
Lipid interaction research: Due to its origin within a domain of apoE known for lipid association, this peptide fragment is instrumental in studies examining the mechanisms of lipid binding and transport. Researchers employ the 133-149 segment to probe the biophysical interactions between apolipoprotein E and various lipid species, including phospholipids and cholesterol. Such investigations help clarify the contribution of this sequence to lipoprotein particle assembly, lipid solubilization, and membrane association, providing essential insights into the molecular basis of lipid metabolism and transport.
Neurobiological investigations: The apoE(133-149) peptide serves as a valuable probe in neurobiology, particularly in the context of neurodegenerative disease models and neuronal signaling. The fragment's sequence encompasses residues implicated in modulating synaptic function, amyloid-beta interactions, and cellular signaling pathways relevant to neurological health. By incorporating this peptide into in vitro or ex vivo systems, researchers can assess its effects on neuronal receptor modulation, aggregation phenomena, or the regulation of neurotoxic species, thereby advancing understanding of apoE's role in central nervous system physiology.
Protein structure-function analysis: In structural biology and protein engineering, the apoE(133-149) peptide is frequently applied to investigate the conformational dynamics and functional motifs of the parent protein. Its defined length and sequence facilitate detailed studies using techniques such as circular dichroism, NMR spectroscopy, or crystallography, enabling the characterization of secondary structure elements and interaction surfaces. These analyses are essential for mapping functional domains within apoE, guiding the rational design of peptide mimetics or inhibitors, and elucidating the structural underpinnings of protein-ligand recognition.
Peptide-based assay development: The well-characterized nature of the 133-149 fragment makes it a preferred standard in the development and optimization of peptide-based analytical assays. It can be employed as a reference substrate or binding partner in ELISA, fluorescence polarization, or surface plasmon resonance platforms, supporting the quantification of receptor interactions, antibody specificity, or competitive inhibition. Its reproducibility and defined sequence allow for consistent assay calibration and comparative studies, enhancing the reliability of experimental workflows in lipid metabolism and neurobiology research.
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