Synthesis of a triply phosphorylated pentapeptide from human τ-protein
| Autor: | Oliver Seitz, Thomas Zelinski, Norman Kuder, Herbert Waldmann, Tanmaya Pathak |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Phosphopeptides
Magnetic Resonance Spectroscopy Stereochemistry Clinical Biochemistry Pharmaceutical Science tau Proteins Peptide Tripeptide Biochemistry Pentapeptide repeat Chemical synthesis Serine chemistry.chemical_compound Drug Discovery Peptide synthesis Humans Molecular Biology chemistry.chemical_classification Molecular Structure Phosphopeptide Organic Chemistry Peptide Fragments Amino acid Models Chemical chemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Molecular Medicine |
| Zdroj: | Bioorganic & Medicinal Chemistry. 8:2433-2439 |
| ISSN: | 0968-0896 |
| DOI: | 10.1016/s0968-0896(00)00174-7 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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