CAJ | 학술논문

目的：研究姜黄素对Hsp90的结合及抑制作用。方法：采用分子模拟对接、等温滴定微量热法及Oc-tet技术检测姜黄素与Hsp90的结合机制。采用变性荧光素酶再复性法检测姜黄素对Hsp90的抑制作用。结果：分子模拟对接结果显示姜黄素与Hsp90的ATPase区域有特异性结合。等温滴定微量热法及Octet测定二者的结合常数分别为2.84×104L/mol和9.79×104L/mol。荧光素酶复性法确定姜黄素能通过对 Hsp90的抑制作用阻止其对变性荧光素酶进行修复，与阳性对照 GA 相比（ IC50值为1.14μmol/L），姜黄素对Hsp90的IC50值为7.51μmol/L。结论：姜黄素与Hsp90有较强的结合且对其分子伴侣功能具有一定的抑制效果。
목적：연구강황소대Hsp90적결합급억제작용。방법：채용분자모의대접、등온적정미량열법급Oc-tet기술검측강황소여Hsp90적결합궤제。채용변성형광소매재복성법검측강황소대Hsp90적억제작용。결과：분자모의대접결과현시강황소여Hsp90적ATPase구역유특이성결합。등온적정미량열법급Octet측정이자적결합상수분별위2.84×104L/mol화9.79×104L/mol。형광소매복성법학정강황소능통과대 Hsp90적억제작용조지기대변성형광소매진행수복，여양성대조 GA 상비（ IC50치위1.14μmol/L），강황소대Hsp90적IC50치위7.51μmol/L。결론：강황소여Hsp90유교강적결합차대기분자반려공능구유일정적억제효과。
Objective:To study the binding and inhibition function of Curcumin on Hsp90. Methods:Molecular docking,isothermal titration calorimetry and octet assay were used to estimate the binding ability of Curcumin to Hsp90. Denatured firefly luciferase renature assay was used to confirm the inhibition function of Curcumin to Hsp90. Results:Molecular result showed that Curcumin is able to bind to the ATPase domain of Hsp90 specificly,and the binding constants were 2. 84 × 104 L/mol for isathermal titration calorimetry assayand 9. 79 × 104 L/mol for Octet assay respectively. Renaturation of firefly luciferase refolding assay further comfirmed that Curcumin can prevent Hsp90 for repairing denatured luciferase,the IC50 value was 7. 51μmol/L( IC50 value of Geldanamycin is 1. 14μmol/L). Con-clusion:Curcumin is able to inhibit the chaperone function of Hsp90 by the strong binding ability.