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藥物Tranilast可阻絕S100A12蛋白與V-domain的結合
邱建維 , Masters Advisor：余靖
繁體中文
S100A12 ； RAGE V domain ； 蛋白質作用 ； 蛋白質結構 ； Tranilast ； S100A12 ； RAGE V domain ； Protein-Protein interaction ； Protein Structure ； Tranilast
- Abstract
- S100A12 (Calgranuline C) is a small and dimeric protein which belongs to the S100 family. When calcium ions bind to the two EF-hands of S100A12, the protein structure changes and promotes the interaction with its target proteins. RAGE (receptor for advanced glycation end) is one of the target protein for S100A12. By the past research, it showed the binding between these two proteins generated a pro-inflammatory response and activated several signal pathways such as ERK and NF-κB. It is an effective way that preventing the formation of S100A12-RAGE protein complex to inhibit various cancers.
- Tranilast, an anti-allergic drug that is usually used as treatment of allergic disorders, was found to have a strong interaction with S100A12 which may be a potential inhibitor. In this study, we discussed the interaction of S100A12 with RAGE and S100A12 with tranilast by their three dimension structure. We utilized several biophysical techniques, including multidimensional NMR spectroscopy, fluorescence spectroscopy, HADDOCK and WST-1 assay to characterize the structural information of protein complex.
- This study describes structural properties of S100A12-tranilast and S100A12-RAGE complex. It shows that tranilast blocks the binding sites of S100A12- RAGEV. This result can be useful for the development of new drug against various diseases.
