人體纖維母細胞生長因子(FGF)在細胞中所調節的機制過程非常廣泛,其生物活性主要是藉由和細胞表面受體(FGF receptor)之間的結合來傳達.在本研究當中,我們已經成功地利用大腸桿菌(E. coli)將表面受體中的第二功能區塊(domain 2)蛋白表達出來,並經由各種純化步驟得到大量的高純度蛋白.在蛋白質結構的初步鑑定上,經由圓二色光譜儀(circular dichroism, CD)和化學位移預測法(chemical shift index, CSI)我們可以得知, 第二功能區塊蛋白主要是由9個β摺板(β-sheet)所組成.至於第二功能區塊蛋白的生物活性,則是透過恆溫滴定熱卡計(isothermal titration calorimetry, ITC)和尿素變性實驗(Urea-induced denaturation),來加以證實第二功能區塊蛋白和配體(ligand,包括FGF, heparin和SOS)之間的結合作用力.
此外,我們亦根據在核磁共振(NMR)實驗上所得之數據,經由電腦計算的方式(ARIA-CNS)將第二功能區塊蛋白在水溶液中的三度空間結構(three-dimensional structure)解出,以便研究第二功能區塊蛋白與配體之間的相互作用力,並進一步透過化學位移擾動(chemical shift perturbation)實驗來找出參與結合的殘基位置(binding site),達到將結合作用區域最小化(minimization)的目的.所得到的結果,將會在藥物開發和相關疾病治療上有相當的貢獻.另一方面,在蛋白質分子狀態(molecular state)得探討上,我們利用高速中壓色層分析系統(fast performance liquid chromatography, FPLC)來偵測第二功能區塊蛋白本身以及與配體之間的結合/分離狀態 (association/dissociation state),以便進一步了解人體纖維母細胞生長因子之系統活化過程.

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