Synthesis and evaluation of acyl protein thioesterase 1 (APT1) inhibitors |
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Authors: | Biel Markus Deck Patrick Giannis Athanassios Waldmann Herbert |
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Affiliation: | University of Leipzig, Institute of Organic Chemistry, Johannisallee 29, 04103 Leipzig, Germany. |
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Abstract: | Lipid-modified proteins play decisive roles in important biological processes such as signal transduction, organisation of the cytoskeleton and vesicular transport. Lipidation of these proteins is essential for correct biological function. Among the modifications with lipids, prenylation and myristoylation are well understood. However, the machinery of palmitoylation is still under investigation. Recently, an enzyme, acyl protein thioesterase 1 (APT1), that may play a regulatory role in the palmitoylation cycle of H-Ras and G-protein alpha subunits, was purified. Motivated by this work, several inhibitors of APT1 were designed, synthesized and biologically evaluated leading to highly active compounds. |
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Keywords: | palmitoylation peptidomimetics proteins signal transduction |
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