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【公司名稱】 廣州健侖生物科技有限公司
【】    楊永漢 
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研究結(jié)果已發(fā)表在JouRNAl of Controlled Release雜志上，目前研究仍然處于早期階段，接下來的步驟是通過小鼠體內(nèi)試驗(yàn)來測試其功效。
自從1969年已故諾貝爾獎得主Dorothy C. Hodgkin闡明胰島素的存儲結(jié)構(gòu)以來，胰島素已經(jīng)改善了世界上5億多人糖尿病患者的健康，并延長了他們的壽命。病患者的健康，并延長了他們的壽命。然而，這種關(guān)鍵激素如何與身體器官中的靶細(xì)胞結(jié)合?
現(xiàn)在，由Michael A. Weiss博士(克里夫蘭凱斯西儲大學(xué)醫(yī)學(xué)院)和Michael C. Lawrence博士(沃爾特和伊萊扎研究所和澳大利亞墨爾本大學(xué))共同的研究小組，解釋了胰島素分子如何利用一種“保護(hù)鉸鏈”來參與胰島素受體內(nèi)的主要結(jié)合位點(diǎn)。相關(guān)文章發(fā)表于2014年8月4日的《PNAS》雜志上。
在本次調(diào)查研究中，Weiss、Lawrence及其同事們在胰島素內(nèi)發(fā)現(xiàn)了一個保護(hù)鉸鏈，當(dāng)它關(guān)閉時，可確保激素存儲為一種安全的形式，直到它適時地打開——這種結(jié)構(gòu)的轉(zhuǎn)變可允許其對接到肌肉、肝臟、脂肪和其他組織靶細(xì)胞的表面。這種對接是代謝信號的*步，例如，這可使靶細(xì)胞能夠吸收葡萄糖(糖構(gòu)建模塊)，從而避免血液中葡萄糖的積聚(高血糖)——糖尿病的基本特征。
研究人員通過觀察晶體結(jié)構(gòu)(在其構(gòu)建模塊中，一個單一的胰島素分子結(jié)合到胰島素受體片段上)中可視化的復(fù)雜結(jié)構(gòu)特征，發(fā)現(xiàn)了保護(hù)性鉸鏈。過去的研究，包括胰島素結(jié)構(gòu)Hodgkin在內(nèi)，都集中在缺乏受體的6個胰島素分子組(六聚體)。這種封閉形式的胰島素，關(guān)系到它如何存儲在體內(nèi)或制備在藥物制劑中。六聚體含有三對胰島素分子(二聚體)。每個二聚體包含八個芳香環(huán)的交叉點(diǎn)，四個來自每個胰島素分子。(芳香環(huán)是分子內(nèi)的碳原子形成的閉環(huán)結(jié)構(gòu))。在激素開放和活躍形式的新圖像中，這些芳香環(huán)駐留在細(xì)胞受體的口袋內(nèi)。因此，胰島素打開一個鉸鏈，接觸其功能表面。
Weiss稱：“我們相信，胰島素的關(guān)閉形式進(jìn)化到允許其高效地生產(chǎn)并儲存在胰腺內(nèi)。然而，在這種狀態(tài)下穩(wěn)定的胰島素變異形式，沒有生物活性。”

The findings, published in the JouRNAl of Controlled Release, are still in their early stages and the next step is to test their efficacy in mice in vivo.
Since the late 1969 Nobel laureate Dorothy C. Hodgkin clarified the structure of insulin stores, insulin has improved the health and long-lived lives of more than 500 million people with diabetes in the world. The sick's health and prolong their life expectancy. However, how does this key hormone bind to target cells in body organs?
Now a team led by Dr. Michael A. Weiss (Case Western Reserve University of Cleveland) and Dr. Michael C. Lawrence (Walter & Eliza Institute and University of Melbourne, Australia) explained that insulin molecules How to use a "protective hinge" to participate in the major binding sites within the insulin receptor. The article was published in PNAS magazine on August 4, 2014.
In this study, Weiss, Lawrence, and colleagues found a protective hinge within insulin that when stored, ensures that hormones are stored in a safe form until it opens in a timely fashion - The transition allows it to dock to the surface of muscle, liver, fat and other tissue target cells. This docking is the first step in the metabolic signal, for example, which allows the target cells to absorb glucose (sugar building blocks) and thus avoids the accumulation of glucose in the blood (hyperglycemia), the essential feature of diabetes.
The researchers found protective hinges by looking at the complex structural features that are visualized in the crystal structure (in which a single insulin molecule binds to the insulin receptor fragment in its building block). Past research, including insulin structural pioneer Hodgkin, has focused on the six insulin molecule sets (hexamers) lacking the receptor. This closed form of insulin is related to how it is stored in the body or prepared in a pharmaceutical formulation. Hexamers contain three pairs of insulin molecules (dimers). Each dimer contains the intersection of eight aromatic rings and four from each insulin molecule. (Aromatic rings are closed-loop structures formed by intramolecular carbon atoms). In new images of hormone-opening and active forms, these aromatic rings reside in the pockets of cellular receptors. Therefore, insulin opens a hinge that contacts its functional surface.
"We believe the closed form of insulin evolved to allow it to be efficiently produced and stored within the pancreas," said Weiss, however, the steady variant forms of insulin in this state are not biologically active. "