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dc.contributor.authorJones, Sarah
dc.contributor.authorOstlund, Pernilla
dc.contributor.authorLangel, Ulo
dc.contributor.authorZorko, Matjaz
dc.contributor.authorNicholl, Iain D.
dc.contributor.authorHowl, John D.
dc.date.accessioned2008-06-20T16:15:03Z
dc.date.available2008-06-20T16:15:03Z
dc.date.issued2006
dc.identifier.citationJones, S., Östlund, P., Langel, Ü., Zorko, M., Nicholl, I.D., & Howl, J. (2006). A rhegnylogic strategy for the synthesis of signal transduction modulatory, cell penetrating peptides. Poland, Gdansk: Wiley InterScience
dc.identifier.isbn9789655552973
dc.identifier.issn1075-2617
dc.identifier.issn1099-1387
dc.identifier.urihttp://hdl.handle.net/2436/30273
dc.description.abstractINTRODUCTION: Many cell-penetrating peptides (CPP) have been utilised as biologically inert vectors. A majority of these studies employ sychnologically organised constructs in which a bioactive cargo (message) is chemically conjugated to the CPP (address). Previously, we have adopted a sychnologic strategy to modulate intracellular signal transduction. Using chimeric constructs composed of the CPP transportan 10, conjugated to partial sequences that correspond to functional domains of signal transduction proteins, we have selectively modulated a variety of cellular activities including secretion and activation of p42/p44 mitogen-activated protein kinases [1, 2]. However, a QSAR-based algorithm can now be used to predict CPP that reside within the primary sequences of proteins [3]. We have adapted this strategy to identify CPP within signal transducing proteins including functional domains that govern protein-protein interactions. Data presented herein indicate that it is now feasible to identify rhegnylogic sequences, containing vectoral-independent discontinuously organised pharmacophores, that are cell penetrant modulators of signal transduction pathways.
dc.formatapplication/pdf
dc.language.isoen
dc.publisherWiley InterScience
dc.relation.urlhttps://onlinelibrary.wiley.com/toc/10991387/2006/12/S1
dc.subjectPeptides
dc.subjectCPP
dc.subjectCell Penetrating Peptides (CPP)
dc.subjectSignal Transduction
dc.subjectMolecular Biology
dc.subjectRhegnylogic strategy
dc.subjectChimerism
dc.titleA rhegnylogic strategy for the synthesis of signal transduction modulatory, cell penetrating peptides
dc.title.alternativeIn: Rolka, R., Rekowski, P. & Siberring, J. (Eds.), Peptides 2006 : Proceedings of the Twenty-Ninth European Peptide Symposium, Gdansk, Poland, 3 - 8 Sept. 2006, No. 0212
dc.typeConference contribution
dc.identifier.journalJournal of Peptide Science
refterms.dateFOA2020-03-09T09:55:39Z
html.description.abstractINTRODUCTION: Many cell-penetrating peptides (CPP) have been utilised as biologically inert vectors. A majority of these studies employ sychnologically organised constructs in which a bioactive cargo (message) is chemically conjugated to the CPP (address). Previously, we have adopted a sychnologic strategy to modulate intracellular signal transduction. Using chimeric constructs composed of the CPP transportan 10, conjugated to partial sequences that correspond to functional domains of signal transduction proteins, we have selectively modulated a variety of cellular activities including secretion and activation of p42/p44 mitogen-activated protein kinases [1, 2]. However, a QSAR-based algorithm can now be used to predict CPP that reside within the primary sequences of proteins [3]. We have adapted this strategy to identify CPP within signal transducing proteins including functional domains that govern protein-protein interactions. Data presented herein indicate that it is now feasible to identify rhegnylogic sequences, containing vectoral-independent discontinuously organised pharmacophores, that are cell penetrant modulators of signal transduction pathways.


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