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A rhegnylogic strategy for the synthesis of signal transduction modulatory, cell penetrating peptides
Jones, Sarah Ostlund, Pernilla Langel, Ulo Zorko, Matjaz Nicholl, Iain D. Howl, John D.
Jones, Sarah
Ostlund, Pernilla
Langel, Ulo
Zorko, Matjaz
Nicholl, Iain D.
Howl, John D.
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2006
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In: 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
Abstract
INTRODUCTION: 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.
Citation
Jones, 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
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en
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1075-2617
1099-1387
1099-1387
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9789655552973