Control peptide version of dynamin inhibitory peptide, myristoylated. It is an inhibitor of the GTPase dynamin that competitively blocks binding of dynamin to amphiphysin, preventing endocytosis.
CAT No: R0848
CAS No:251634-22-7
Synonyms/Alias:251634-22-7;AKOS024456771;Dynamin inhibitory peptide,myristoylated;PD079118;G13348;S-251634-22-7;
Dynamin inhibitory peptide, myristoylated is a synthetic peptide derivative designed to specifically target and modulate the activity of dynamin, a GTPase enzyme essential for membrane fission events in eukaryotic cells. The peptide is chemically myristoylated, enhancing its membrane association and cellular uptake, thereby increasing its functional potency in experimental systems. As a tool compound, it holds particular significance in cell biology and neurobiology research, enabling precise interrogation of dynamin-dependent processes such as endocytosis, vesicular trafficking, and synaptic vesicle recycling. Its sequence is engineered to mimic the amphiphysin SH3-binding domain, providing selective inhibition of dynamin's interactions and catalytic function without broadly perturbing other GTPases or membrane-remodeling proteins.
Endocytosis research: The myristoylated dynamin inhibitory peptide is widely employed to dissect the molecular mechanisms underlying clathrin-mediated endocytosis. By competitively inhibiting dynamin's GTPase activity, the peptide allows researchers to transiently block vesicle scission from the plasma membrane, facilitating studies of cargo internalization, receptor trafficking, and the temporal dynamics of endocytic events. Its reversible and specific mode of action makes it an invaluable tool for differentiating dynamin-dependent pathways from alternative endocytic routes.
Synaptic vesicle cycling studies: In neurobiology, the peptide is utilized to probe the role of dynamin in synaptic vesicle endocytosis and recycling. Application of the inhibitor in neuronal cultures or ex vivo preparations enables precise temporal control over synaptic vesicle retrieval following neurotransmitter release. This approach aids in elucidating the contribution of dynamin-mediated fission to synaptic plasticity, neurotransmission fidelity, and the maintenance of synaptic vesicle pools.
Membrane trafficking analysis: The compound serves as a critical reagent in the broader study of intracellular membrane trafficking, including the formation and maturation of endosomes, lysosomes, and other vesicular compartments. By selectively impeding dynamin function, researchers can investigate the consequences for organelle biogenesis, cargo sorting, and the spatial organization of membrane networks, providing insights into the coordination of trafficking events in both physiological and pathological contexts.
Peptide-protein interaction assays: The myristoylated peptide is also valuable in biochemical and biophysical studies aimed at characterizing dynamin's binding partners and regulatory interactions. Its defined sequence and inhibitory properties make it suitable for in vitro assays such as pull-downs, surface plasmon resonance, or fluorescence polarization, where it can be used to competitively displace endogenous ligands or to validate the specificity of dynamin-targeting small molecules and antibodies.
Peptide delivery and cellular uptake research: The myristoylation of the peptide not only enhances its membrane affinity but also serves as a model system for studying lipid-modified peptide delivery strategies. Researchers leverage this compound to investigate the efficiency, kinetics, and cellular distribution of myristoylated peptides, informing the design of next-generation cell-penetrating peptides and targeted delivery vehicles for experimental modulation of intracellular pathways.
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