PKI (14-22) amide (myristoylated) is cell-permeable protein kinase A inhibitor. The non-myristoylated type of this peptide is a highly specific inhibitor of cAMP-dependent protein kinase (PKA), N-terminus is myristoylated to increase cell membrane permeability. It is usually used to study PKA in cellular systems in-vitro.
CAT No: R0879
CAS No:201422-03-9
Synonyms/Alias:201422-03-9;myr-PKI;L-Isoleucinamide,N-(1-oxotetradecyl)glycyl-L-arginyl-L-threonylglycyl-L-arginyl-L-arginyl-L-asparaginyl-L-alanyl-;(2S)-N-[(2S)-1-[[(2S,3S)-1-amino-3-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-2-[[(2S)-5-(diaminomethylideneamino)-2-[[(2S)-5-(diaminomethylideneamino)-2-[[2-[[(2S,3R)-2-[[(2S)-5-(diaminomethylideneamino)-2-[[2-(tetradecanoylamino)acetyl]amino]pentanoyl]amino]-3-hydroxybutanoyl]amino]acetyl]amino]pentanoyl]amino]pentanoyl]amino]butanediamide;GRTGRRNAI;GTPL10619;AKOS024457159;PKI 14-22 amide,myristoylated TFA;AS-86161;DA-56914;G12951;MYR-GRTGRRNAI-NH2 PROTEIN KINASE A INHIBITOR 14-22 AMIDE;(S)-N1-((S)-1-(((2S,3S)-1-Amino-3-methyl-1-oxopentan-2-yl)amino)-1-oxopropan-2-yl)-2-((2S,5S,11S,14S)-2,5,14-tris(3-guanidinopropyl)-11-((R)-1-hydroxyethyl)-4,7,10,13,16,19-hexaoxo-3,6,9,12,15,18-hexaazadotriacontanamido)succinamide;
PKI 14-22 amide, myristoylated is a synthetic peptide inhibitor that incorporates a myristoyl group at the N-terminus, enhancing its cell permeability and functional potency. As a fragment derived from the protein kinase inhibitor (PKI) sequence, this compound is engineered to mimic the natural inhibitory domain targeting cAMP-dependent protein kinase (PKA). The addition of the myristoyl modification enables improved membrane association, making it particularly valuable for in vitro and cell-based studies where intracellular delivery and effective kinase inhibition are required. Researchers utilize this peptide to dissect PKA-mediated signaling pathways, investigate phosphorylation-dependent cellular processes, and evaluate kinase activity modulation with high specificity.
Kinase activity inhibition: As a potent and selective inhibitor of PKA, the myristoylated PKI 14-22 amide peptide is widely used to block PKA catalytic activity in biochemical assays and cell-based experiments. Its sequence is optimized to bind competitively to the catalytic subunit of PKA, preventing substrate phosphorylation and downstream signaling events. This enables researchers to delineate the direct effects of PKA inhibition on various biological processes, such as gene expression regulation, metabolic control, and synaptic plasticity.
Signal transduction research: The compound serves as a powerful tool for probing cAMP/PKA-dependent signaling cascades. By selectively attenuating PKA activity, it allows scientists to investigate the role of cAMP-mediated phosphorylation in diverse cellular contexts, including neuronal signaling, cardiac function, and endocrine regulation. The myristoylation facilitates cellular uptake, ensuring efficient delivery to intracellular targets and enhancing the reliability of mechanistic studies.
Peptide-based functional assays: In the context of peptide research, myristoylated PKI 14-22 amide is frequently employed in functional assays designed to assess the specificity and efficacy of kinase inhibitors. Its well-characterized inhibitory profile makes it a benchmark control for validating new compounds or screening for modulators of PKA activity. The peptide's structural features also provide a model for developing next-generation peptide inhibitors with improved pharmacological properties.
Cellular localization studies: The myristoyl modification not only aids in membrane association but also enables studies on the subcellular localization of peptide inhibitors. Researchers utilize this property to examine the dynamics of PKA inhibition within different cellular compartments, such as the cytosol, nucleus, or membrane microdomains. Insights gained from these experiments contribute to a deeper understanding of compartmentalized kinase signaling and its physiological implications.
Mechanistic pathway elucidation: The specificity of PKI 14-22 amide, myristoylated, for PKA allows for precise dissection of signaling pathways where multiple kinases may be involved. By selectively inhibiting PKA, researchers can differentiate between PKA-dependent and independent mechanisms in complex biological systems. This capability is particularly valuable in studies aiming to unravel cross-talk between signaling networks, map phosphorylation events, or identify novel regulatory nodes within cellular pathways.
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