Myristoylated form of Pep2m; Cell-permeable inhibitor of the interaction between AMPA receptor and N-ethylmaleimide-sensitive fusion protein (NSF).
CAT No: R1029
Synonyms/Alias:1423381-07-0;AKOS024457808;PD079617;
Chemical Name:(2S)-5-amino-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-(tetradecanoylamino)hexanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-4-methylsulfanylbutanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]propanoyl]amino]hexanoyl]amino]-4-oxobutanoyl]amino]propanoyl]amino]-5-oxopentanoic acid
Pep2m, myristoylated, is a synthetic peptide derivative featuring an N-terminal myristoylation modification, which enhances its membrane affinity and biological activity. As a cell-permeable peptide, Pep2m is specifically engineered to facilitate the intracellular delivery of molecular cargo, including proteins and nucleic acids, by exploiting natural lipid modification pathways. Its design is rooted in the principles of peptide-mediated translocation, making it a valuable tool for researchers investigating cellular uptake mechanisms, protein-protein interactions, and intracellular signaling dynamics. The myristoylation motif not only augments its bioavailability but also imparts unique biophysical properties that are highly relevant in the study of membrane-associated processes.
Cellular delivery studies: Myristoylated Pep2m is widely employed in research focused on enhancing the intracellular uptake of bioactive molecules. Its lipid modification enables efficient translocation across cell membranes, providing a model system for investigating the mechanisms of peptide-mediated delivery. Researchers utilize this peptide to assess the efficiency of cell-penetrating sequences and to optimize protocols for delivering therapeutic candidates, fluorescent probes, or other macromolecules into living cells. Its robust membrane-associating properties enable comparative studies with non-lipidated analogs, yielding critical insights into the role of myristoylation in cellular import.
Protein-protein interaction mapping: The peptide serves as a versatile probe for dissecting interactions between membrane-associated proteins and their cytosolic partners. By mimicking naturally myristoylated signaling motifs, it allows scientists to characterize binding affinities, map interaction domains, and elucidate the molecular determinants of subcellular localization. Its use in pull-down assays, co-immunoprecipitation, and surface plasmon resonance experiments supports the identification of critical protein interfaces, advancing the understanding of signal transduction pathways and membrane recruitment events.
Membrane trafficking research: In the context of vesicular transport and membrane dynamics, myristoylated Pep2m is instrumental for modeling the behavior of lipid-modified proteins. Researchers employ it to study the sorting, compartmentalization, and trafficking of myristoylated cargo within cellular organelles. Its structural mimicry of native lipidated peptides aids in the evaluation of endocytosis, exocytosis, and intracellular routing, providing a controllable system for dissecting the influence of lipid modifications on protein mobility and membrane association.
Peptide functionalization and conjugation studies: The unique chemical properties of myristoylated Pep2m make it a preferred scaffold for the development of multifunctional peptide conjugates. Scientists leverage its reactive sites to attach fluorescent dyes, affinity tags, or therapeutic payloads, enabling the creation of customized molecular tools for imaging, tracking, or targeted delivery. Its compatibility with a range of bioconjugation chemistries facilitates the exploration of structure-activity relationships and the optimization of peptide-based delivery vectors.
Signal transduction modeling: The peptide is also valuable for simulating the initial steps of myristoylation-dependent signaling cascades. By serving as a surrogate for endogenous signaling peptides, it allows for the controlled investigation of activation, recruitment, and downstream effector interactions in vitro and in cell-based systems. Researchers utilize it to probe the effects of lipidation on kinase activation, scaffold assembly, and the spatial organization of signaling complexes, thereby contributing to a deeper mechanistic understanding of myristoylation's role in cellular communication.
2. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
3. Implications of ligand-receptor binding kinetics on GLP-1R signalling
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