Investigation of the protein alkylation sites of the STAT3:STAT3 inhibitor Stattic by mass spectrometry
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 and Thurston, David E.
(2013)
Investigation of the protein alkylation sites of the STAT3:STAT3 inhibitor Stattic by mass spectrometry.
Bioorganic and Medicinal Chemistry Letters (16).
pp. 4719-4722.
ISSN 0960-894X
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.
Item Type | Article |
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Date Deposited | 29 May 2025 09:11 |
Last Modified | 29 May 2025 09:11 |