อันตรกิริยาระหว่างเคอร์คิวมินกับทูเมอร์เนคโครซิสแฟคเตอร์-อัลฟา
Tumor necrosis factor alpha (TNF-α) is a cytokine secreted by macrophage that can causeinflammation and mediate inflammation-related diseases. Currently, investigation of TNF-α inhibitors has been received considerable attention and a number of anti-TNF-α monoclonal antibodies e.g. infliximab, etane...
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Main Authors: | , , |
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Other Authors: | |
Format: | Senior Project |
Language: | Thai |
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จุฬาลงกรณ์มหาวิทยาลัย
2014
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Online Access: | https://digiverse.chula.ac.th/Info/item/dc:9362 |
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Institution: | Chulalongkorn University |
Language: | Thai |
Summary: | Tumor necrosis factor alpha (TNF-α) is a cytokine secreted by macrophage that can causeinflammation and mediate inflammation-related diseases. Currently, investigation of TNF-α inhibitors has been received considerable attention and a number of anti-TNF-α monoclonal antibodies e.g. infliximab, etanercept and adalimumab has been used as anti-inflammatory drugs for the treatment of autoimmune diseases. Recently, curcumin, a polyphenolic compound, has been shown to interact with TNF-α using molecular docking, which could be further developed as a TNF-α inhibitor. However, there is no experimental evidence on the interaction between curcumin and TNF-α. In this work, we therefore investigated the interaction between curcumin and TNF-α using spectrofluorometry. The excitationwavelength was set at 280 nm and the emission spectra of TNF-α were collected from 300 to 400 nm in the presence of various concentrations from 0.4-8.0 uM of curcumin. The results showed that curcumin decreased the fluorescence intensity at 315 nm of TNF-α through the static process. The binding constants, calculated by modified Stern-Volmer equation, were found to be 1.02, 1.13 and 1.38 x 10 M and the number of binding sites, calculated by Stern-Volmer equation, was 0.80, 0.89 and 0.84 at the temperatures of 293, 299 and 305 K, respectively. The thermodynamic parameters, which are enthalpy(ΔH), entropy (Δ5) and Gibbs free energy (ΔG), were calculated from the van t Hoff equation. The values of ΔH and ΔS were greater than O, suggesting that curcumin bound to TNF-α via hydrophobic force and the value of ΔG was less than 0, indicating that the interaction occurs spontaneously. These findings suggest that curcumin has a potential to be developed as anti-TNF-α for therapeutic and biomedical research applications. |
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