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This article is an orphan, as few or no other articles link to it. Please introduce links to this page from related articles; suggestions may be available. (February 2009) Pepducins are novel cell-penetrating peptides that act as intracellular inhibitors of signal transference from receptors to G proteins. Pepducins were first developed at the Tufts Medical Center laboratories of Dr. Athan Kuliopulos and Dr. Lidija Covic [1]. Pepducins utilize lipidated fragments of intracellular G protein-coupled receptor loops to modulate GPCR action in targeted cell-signaling pathways [2]. The Pepducin molecule comprises a short peptide derived from a GPCR intracellular loop tethered to a hydrophobic moiety. This structure allows Pepducin lipopeptides to anchor in the cell membrane lipid bilayer and target the GPCR/G protein interface via a unique intracellular allosteric mechanism. Pepducins for over 15 different GPCRs have been successfully produced, several of which have shown activity in preclinical in vivo models. [3] References ^ Covic L, Gresser AL, Talavera J, Swift S, Kuliopulos A (January 2002). "Activation and inhibition of G protein-coupled receptors by cell-penetrating membrane-tethered peptides". Proc. Natl. Acad. Sci. U.S.A. 99 (2): 643–8. doi:10.1073/pnas.022460899. PMID 11805322.  ^ Kuliopulos A, Covic L (December 2003). "Blocking receptors on the inside: pepducin-based intervention of PAR signaling and thrombosis". Life Sci. 74 (2-3): 255–62. doi:10.1016/j.lfs.2003.09.012. PMID 14607253. http://linkinghub.elsevier.com/retrieve/pii/S0024320503008312.  ^ Kubo S, Ishiki T, Doe I, et al. (December 2006). "Distinct activity of peptide mimetic intracellular ligands (pepducins) for proteinase-activated receptor-1 in multiple cells/tissues". Ann. N. Y. Acad. Sci. 1091: 445–59. doi:10.1196/annals.1378.087. PMID 17341635.