Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 477, Issue 4, Pages 861-867Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2016.06.149
Keywords
Fibroblast growth factor (FGF); Fibroblast growth factor receptor (FGFR); Suramin; Protein purification; NMR solution structure; Protein-ligand interaction; HADDOCK; WST-1 assay
Categories
Funding
- Ministry of Science and Technology (MOST) Taiwan [MOST 103-2113-M-007 -017-MY3, MOST 104-2320-B-039-031]
- China Medical University [CMU104-S-02]
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The extracellular portion of the human fibroblast growth factor receptor2 D2 domain (FGFR2 D2) interacts with human fibroblast growth factor 1 (hFGF1) to activate a downstream signaling cascade that ultimately affects mitosis and differentiation. Suramin is an antiparasitic drug and a potent inhibitor of FGF-induced angiogenesis. Suramin has been shown to bind to hFGF1, and might block the interaction between hFGF1 and FGFR2 D2. Here, we titrated hFGF1 with FGFR2 D2 and suramin to elucidate their interactions using the detection of NMR. The docking results of both hFGF1-FGFR2 D2 domain and hFGF1-suramin complex were superimposed. The results indicate that suramin blocks the interaction between hFGF1 and FGFR2 D2. We used the PyMOL software to show the hydrophobic interaction of hFGF1-suramin. In addition, we used a Water-soluble Tetrazolium salts assay (WST1) to assess hFGF1 bioactivity. The results will be useful for the development of new antimitogenic activity drugs. (C) 2016 Elsevier Inc. All rights reserved.
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