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We recently presented Stafia-1 as the first chemical entity that inhibits the transcription factor STAT5a with selectivity over the highly homologous STAT5b. Stafia-1, which was identified from a series of symmetrically substituted m-terphenyl phosphates, binds to the interface between the SH2 domain and the linker domain of STAT5a. Here, we outline a synthetic strategy for the synthesis of asymmetrically substituted m-terphenyl phosphates, which can be tailored to address their asymmetric STAT5a binding site in a more specific manner. The asymmetrically substituted m-terphenyl phosphate with the highest activity against STAT5a was converted to a phosphatase-stable monofluoromethylene phosphonate. The synthetic methodology and activity analysis described here provide first insights into the structure-activity relationships of m-terphenyl phosphates for use as selective STAT5a inhibitors. © 2021 The Authors. ChemBioChem published by Wiley-VCH GmbH.


Daniel Müller-Klieser, Thorsten Berg. Asymmetrically Substituted m-Terphenyl Phosphates Inhibit the Transcription Factor STAT5a. Chembiochem : a European journal of chemical biology. 2022 Feb 16;23(4):e202100603

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PMID: 34905258

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