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.
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
Metadata
Show full item record