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Journal Article

Synthesis of a triply phosphorylated pentapeptide from human tau-protein

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons98730

Seitz,  Oliver
Abt. IV: Chemische Biologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons98735

Waldmann,  Herbert
Abt. IV: Chemische Biologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Citation

Kuder, N., Zelinski, T., Pathak, T., Seitz, O., & Waldmann, H. (2000). Synthesis of a triply phosphorylated pentapeptide from human tau-protein. BIOORGANIC & MEDICINAL CHEMISTRY, 8(10), 2433-2439. doi:10.1016/S0968-0896(00)00174-7.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-6F0D-F
Abstract
Two different strategies for the synthesis of a triply phosphorylated pentapeptide are described. In both cases a monophosphorylated selectively N-deprotected tripeptide is employed as C-terminal fragment. Coupling of this building block with a C-terminally unmasked bis-phosphorylated seryl-dipeptide unexpectedly failed due to decomposition of this peptide upon activation with different coupling reagents. Instead stepwise N-terminal elongation of the peptide chain with serine derivatives and subsequent O-phosphorylation of the serine OH-groups was successful. These results indicate that assembly of multiply phosphorylated peptides from preformed multiply phosphorylated phosphopeptide building blocks in general may be problematic and that a stepwise elongation of the amino acid chain may be preferable. (C) 2000 Elsevier Science Ltd. All rights reserved.