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

        Author
        Heidelberger, Sibylle
        Zinzalla, Giovanna
        Antonow, Dyeison
        Essex, Samantha
        Piku Basu, B.
        Palmer, Jonathan
        Husby, Jarmila
        Jackson, Paul J. M.
        Rahman, Khondaker M.
        Wilderspin, Andrew F.
        Zloh, Mire
        Thurston, David E.
        Attention
        2299/11798
        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.
        Publication date
        2013-08-15
        Published in
        Bioorganic and Medicinal Chemistry Letters
        Published version
        https://doi.org/10.1016/j.bmcl.2013.05.066
        Other links
        http://hdl.handle.net/2299/11798
        Relations
        School of Life and Medical Sciences
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