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Investigation of the protein alkylation sites of the STAT3:STAT3 inhibitor Stattic by mass spectrometry

Research output: Contribution to journalArticle

Sibylle Heidelberger, Giovanna Zinzalla, Dyeison Antonow, Samantha Essex, B Piku Basu, Jonathan Palmer, Jarmila Husby, Paul J M Jackson, Khondaker M Rahman, Andrew F Wilderspin, Mire Zloh, David E Thurston

Original languageEnglish
Pages (from-to)4719-4722
Number of pages4
JournalBIOORGANIC AND MEDICINAL CHEMISTRY LETTERS
Volume23
Issue number16
Early online date29 May 2013
DOIs
E-pub ahead of print29 May 2013
Published15 Aug 2013

Bibliographical note

Copyright © 2013. Published by Elsevier Ltd.

King's Authors

Abstract

STAT3 (Signal Transducer and Activator of Transcription factor 3) is constitutively active in a wide range of human tumours. Stattic is one of the first non-peptidic small molecules reported to inhibit formation of the STAT3:STAT3 protein dimer complex. A mass spectrometry method has been developed to investigate the binding of Stattic to the un-phosphorylated STAT3βtc (U-STAT3) protein. Alkylation of four cysteine residues has been observed with possible reaction at a fifth which could account for the mechanism of action.

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