Synlett 2017; 28(15): 1917-1922
DOI: 10.1055/s-0036-1590834
© Georg Thieme Verlag Stuttgart · New York

Chemical Synthesis of the Multiply Phosphorylated and Biotinylated N-Terminal Transactivation Domain of Human p53 (p53TAD)

Xiaoyang Guana, Patrick K. Chaffeya, Yuan Ruana, Connor K. Hurda, Dylan J. Taatjesb, Zhongping Tan*a
  • aDepartment of Chemistry and Biochemistry and BioFrontiers Institute, University of Colorado, Boulder, CO 80303, USA   Email:
  • bDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80303, USA
This material is based upon work supported by the National Science Foundation under CHE - 1454925.
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Publication History

Received: 30 April 2017

Accepted after revision: 17 June 2017

Publication Date:
20 July 2017 (eFirst)

Published as part of the Cluster Recent Advances in Protein and Peptide Synthesis


Phosphorylation of the N-terminal transactivation domain (TAD) of tumor suppressor p53 (p53TAD) helps regulate many of p53’s biological functions. Chemical synthesis of the p53TAD sequence with various phosphorylation patterns, through native chemical ligation and metal-free desulfurization, would facilitate studies of p53TAD phosphorylation and its role in regulating p53 function. Here, unphosphorylated, mono- and pentaphosphorylated p53TAD constructs were chemically synthesized. During the synthesis, methionine oxidation was found to be a serious problem and reduction was required at different stages, according to the number of phosphorylation sites.

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