Design and synthesis of a peptide derived from positions 195-244 of human cdc25C phosphatase - Université de Montpellier Accéder directement au contenu
Article Dans Une Revue Journal of Peptide Science Année : 1999

Design and synthesis of a peptide derived from positions 195-244 of human cdc25C phosphatase

Résumé

We have designed, synthesized and purified a 51 amino acid peptide derived from an essential domain of human cdc25C phosphatase. In vivo, differential phosphorylation of this domain regulates either the induction of mitotic processes, or the checkpoint arrest of eukaryotic cells in response to DNA damage. Peptide synthesis was achieved using the stepwise Fmoc strategy and resulted in an important yield of highly pure peptide. The final peptide was identified by amino acid analysis, electrospray mass spectrometry and nuclear magnetic resonance, which revealed that one of the two methionines within the peptide was oxidized into its sulphoxide derivative We investigated whether this 51 amino acid peptide folded into secondary structures in solution by circular dichroism and observed the formation of alpha helices in TFE. Finally, we verified that this peptide could bind to its biologically relevant 14-3-3 partner in vitro by fluorescence spectroscopy.

Dates et versions

hal-03149517 , version 1 (23-02-2021)

Identifiants

Citer

May Morris, Jean Mery, Annie Heitz, Frederic Heitz, Gilles Divita. Design and synthesis of a peptide derived from positions 195-244 of human cdc25C phosphatase. Journal of Peptide Science, 1999, 5 (6), pp.263-271. ⟨10.1002/(SICI)1099-1387(199906)5:6<263::AID-PSC191>3.0.CO;2-A⟩. ⟨hal-03149517⟩
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