美國Sercare單增李斯特菌屬特異性陽性對(duì)照

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美國Seracare單增李斯特菌屬特異性陽性對(duì)照

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美國Seracare單增李斯特菌屬特異性陽性對(duì)照

然而，這種強(qiáng)大的“自然武器”目前還不能用于治療，這是由于它的高毒性和缺乏細(xì)胞特異性，它不僅會(huì)損害腫瘤細(xì)胞，也將影響患者的健康細(xì)胞。因此，研究人員設(shè)計(jì)一種手段，以一個(gè)特定的和可控制的方式輸送肽到腫瘤，并使其在腫瘤細(xì)胞中堆積。
該系統(tǒng)由裝載兩個(gè)“組件”的載體聚合物組成：能綁定到腫瘤細(xì)胞受體的肽和黃蜂毒液的毒性肽。體外實(shí)驗(yàn)表明，黃蜂毒液的毒性肽被充分地遞送分布在腫瘤細(xì)胞內(nèi)，并導(dǎo)致其死亡，而正常細(xì)胞如紅細(xì)胞不受影響。
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(jiǎng)得主Dorothy C. Hodgkin闡明胰島素的存儲(chǔ)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(chǔ)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?cè)谝葝u素內(nèi)發(fā)現(xiàn)了一個(gè)保護(hù)鉸鏈，當(dāng)它關(guān)閉時(shí)，可確保激素存儲(chǔ)為一種安全的形式，直到它適時(shí)地打開——這種結(jié)構(gòu)的轉(zhuǎn)變可允許其對(duì)接到肌肉、肝臟、脂肪和其他組織靶細(xì)胞的表面。這種對(duì)接是代謝信號(hào)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(gè)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(gè)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(chǔ)在體內(nèi)或制備在藥物制劑中。六聚體含有三對(duì)胰島素分子(二聚體)。每個(gè)二聚體包含八個(gè)芳香環(huán)的交叉點(diǎn)，四個(gè)來自每個(gè)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(gè)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(chǔ)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。”

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【公司名稱】 廣州健侖生物科技有限公司
【市場部】    楊永漢

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【公司地址】 廣州清華科技園創(chuàng)新基地番禺石樓鎮(zhèn)創(chuàng)啟路63號(hào)二期2幢101-103室

However, this powerful "natural weapon" is currently not available for treatment due to its high toxicity and lack of cell specificity, which not only damages tumor cells but also affects healthy cells in patients. Therefore, the researchers devised a means to deliver the peptide to the tumor in a specific and controlled manner and allow it to accumulate in the tumor cells.
The system consists of a carrier polymer loaded with two "assemblies": a toxic peptide that binds to a tumor cell receptor peptide and wasps venom. In vitro experiments showed that the virulent peptide of the wasp venom is sufficiently delivered to distribute within the tumor cells and cause its death, whereas normal cells such as red blood cells are unaffected.
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) explain 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 metabolic signaling, for example, which allows target cells to absorb glucose (sugar building blocks) and thus avoids the accumulation of glucose in the blood (hyperglycemia), the basic 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. "