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Biochem Biophys Res Commun. 2014 Nov 21;454(3):404-9. doi: 10.1016/j.bbrc.2014.10.048. Epub 2014 Oct 17.

Interaction between S100P and the anti-allergy drug cromolyn.

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Department of Chemistry, National Tsing Hua University, Hsinchu 30013, Taiwan.
Graduate Institute of Cancer Biology and Center for Molecular Medicine, China Medical University, Taichung 404, Taiwan; Department of Biotechnology, Asia University, Taichung 413, Taiwan.
Department of Chemistry, National Tsing Hua University, Hsinchu 30013, Taiwan; The Key Laboratory for Chemical Biology of Fujian Province, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China. Electronic address:


The S100P protein has been known to mediate cell proliferation by binding the receptor for advanced glycation end products (RAGE) to activate signaling pathways, such as the extracellular regulated kinase (ERK) and nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) pathways. S100P/RAGE signaling is involved in a variety of diseases, such as cancer, metastasis, and diabetes. Cromolyn is an anti-allergy drug that binds S100P to block the interaction between S100P and RAGE. In the present study, we characterized the properties of the binding between cromolyn and calcium-bound S100P using various biophysical techniques. The binding affinity for S100P and cromolyn was measured to be in the millimolar range by fluorescence spectroscopy. NMR-HSQC titration experiments and HADDOCK modeling was employed to determine the spatial structure of the proposed heterotetramer model of the S100P-cromolyn complex. Additional MD simulation results revealed the important properties in the complex stability and conformational flexibility of the S100P-cromolyn complex. This proposed model has provided an understanding of the molecular level interactions of S100P-cromolyn complex.


Cromolyn; HADDOCK; HSQC; Molecular dynamics; S100P protein

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