Table of Contents
International Journal of Peptides
Volume 2010, Article ID 189396, 4 pages
Research Article

Synthesis of Peptides from α- and β-Tubulin Containing Glutamic Acid Side-Chain Linked Oligo-Glu with Defined Length

1Department of Chemical Biology, Helmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany
2Departamento de Bioquimica, Universidade Estadual de Campinas, Sao Paulo 13085-135, Brazil
3Synaptic Systems, Inhoffenstraße 7, 38124 Braunschweig, Germany

Received 20 July 2010; Accepted 19 October 2010

Academic Editor: Hubert Vaudry

Copyright © 2010 Werner Tegge et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Side-chain oligo- and polyglutamylation represents an important posttranslational modification in tubulin physiology. The particular number of glutamate units is related to specific regulatory functions. In this work, we present a method for the synthesis of building blocks for the Fmoc synthesis of peptides containing main chain glutamic acid residues that carry side-chain branching with oligo-glutamic acid. The two model peptide sequences CYEEVGVDSVEGEG-E( E 𝑥 )-EEGEEY and CQDATADEQG-E( E 𝑥 )-FEEEEGEDEA from the C-termini of mammalian α1- and β1-tubulin, respectively, containing oligo-glutamic acid side-chain branching with lengths of 1 to 5 amino acids were assembled in good yield and purity. The products may lead to the generation of specific antibodies which should be important tools for a more detailed investigation of polyglutamylation processes.