Journal
JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS
Volume 160, Issue -, Pages 80-88Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jpba.2018.07.018
Keywords
STAT3; Differential scanning fluorimetry; Differential scanning light scattering; Thermal stability assays; Protein truncations
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Funding
- Swedish Society for Medical Research (SSMF)
- David and Astrid Hagelen Foundation (BDGP)
- Swedish Cancer Society
- Swedish Childhood Cancer Society
- Radiumhemmet Research Foundation
- Swedish Research Council
- Karolinska Institute
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STAT3 protein is an established target for the development of new cancer therapeutic agents. Despite lacking a traditional binding site for small molecule inhibitors, many STAT3 inhibitors have been identified and explored for their anti-cancer activity. Because STAT3 signaling is mediated by protein-protein interactions, indirect methods are often employed to determine if proposed STAT3 inhibitors bind to STAT3 protein. While established STAT3 inhibition assays (such as the fluorescence polarization assay, electrophoretic mobility shift assay and ELISAs) have been used to identify novel inhibitors of STAT3 signaling, methods that directly assess STAT3 protein-inhibitor interactions could facilitate the development of novel inhibitors. In this context, we herein report new STAT3 binding assays based on differential scanning fluorimetry (DSF) and differential scanning light scattering (DSLS) to characterize interactions between STAT3 protein and inhibitors. Several peptide and small molecule STAT3 inhibitors have been evaluated, and new insight into how these compounds may interact with STAT3 is provided. (C) 2018 Elsevier B.V. All rights reserved.
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