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The commercially available STAT3 inhibitor 5,15-diphenylporphyrin (5,15-DPP) does not directly interact with STAT3 core residues 127-722.

ABSTRACT:

Objective

Target specific small molecule inhibitors has driven signaling pathway discovery and are used as common positive controls in drug discovery screens. During a biophysical screen, using surface plasmon resonance spectroscopy, of a novel small molecule library for the Signal Transducer and Activator of Transcription 3 Src Homology 2 (STAT3-SH2) low molecular weight interactors we evaluated commercial inhibitors S3I-201 and 5,15-diphenylporphyrin (5, 15-DPP) as positive controls.

Results

Here, we show using surface plasmon resonance spectroscopy that a common STAT3-SH2 inhibitor, 5,15-diphenylporphyrin (5, 15-DPP), does not bind STAT3 core amino acid residues 127 to 722 relative to another commercially available SH2 inhibitor, S3I-201. This finding should provide caution in data interpretation when using 5,15-DPP in in vitro and in vivo laboratory investigations.

SUBMITTER: Mtwebana SS

PROVIDER: S-EPMC7372768 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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The commercially available STAT3 inhibitor 5,15-diphenylporphyrin (5,15-DPP) does not directly interact with STAT3 core residues 127-722.

Mtwebana Siphokazi Sinethemba SS Prinsloo Earl E

BMC research notes 20200720 1

<h4>Objective</h4>Target specific small molecule inhibitors has driven signaling pathway discovery and are used as common positive controls in drug discovery screens. During a biophysical screen, using surface plasmon resonance spectroscopy, of a novel small molecule library for the Signal Transducer and Activator of Transcription 3 Src Homology 2 (STAT3-SH2) low molecular weight interactors we evaluated commercial inhibitors S3I-201 and 5,15-diphenylporphyrin (5, 15-DPP) as positive controls.<h ...[more]

PMID: 32690111

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