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Strategies for phosphatase inhibition and models of biomimetic catalysis.

機(jī)譯：磷酸酶抑制策略和仿生催化模型。

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Enzyme inhibition is a common strategy used to study activity. Effective inhibitors must display specificity and potency to the desired enzyme target. These inhibitors are chemical tools to address questions concerning biological catalysis. In particular, this thesis details two inhibition strategies to study phosphatases, a class of enzymes that catalyze the hydrolysis of phosphate esters. Reversible phosphorylation is now recognized as the pre-eminent mode of cellular communication in biological systems. Understanding the details of enzymecatalyzed phosphate ester hydrolysis may extend our general understanding of how enzymes catalyze chemical reactions.; Many phosphatase inhibitors incorporate functionality to mimic the charge and geometry of the natural phosphorylated substrate. The most direct substitution is replacement of the phosphate moiety by a nonhydrolyzable phosphonate. These derivatives and their analogues are typically poor inhibitors of metallophosphatases. Phosphonic acids bearing pendant ligands are shown to be effective inhibitors of metallophosphatases. In conjunction with inhibitor structure-activity studies, X-ray structure analyses were used to illustrate the various binding modes of two inhibitors to alkaline phosphatase.; Protein-protein interactions govern many biological processes. This thesis describes the synthesis of a site-specific protein modification tool. This tool can be used to probe the importance of these interactions on protein tyrosine phosphatase (PTPase) activity and/or inhibition. These molecules are designed to easily incorporate a PTPase-specific inhibitor motif into a folded protein framework. This displayed inhibitor can now “borrow” the surrounding surface area to increase recognition by PTPases. The described syntheses provide a combinatorial approach to efficiently adjust the specific protein-inhibitor conjugate.; There is a long history of developing artificial catalysts based on enzymatic reaction mechanisms. Many of these efforts have been largely unsuccessful. The catalytic machinery utilized by sulfatases was attached to a cyclodextrin scaffold. This biomimetic model was examined as a catalyst of ester hydrolysis. Additionally, simple aldehyde hydrates were assayed hydrolytic catalysts. Collectively, these chemical methods are designed to further our understanding of enzymatic catalysis.
機(jī)譯：酶抑制是用于研究活性的常用策略。有效的抑制劑必須表現(xiàn)出對(duì)所需酶靶標(biāo)的特異性和效力。這些抑制劑是解決有關(guān)生物催化問題的化學(xué)工具。特別是，本論文詳細(xì)介紹了兩種抑制策略來研究磷酸酶，磷酸酶是一類催化磷酸酯水解的酶?？赡娴牧姿峄F(xiàn)在被認(rèn)為是生物系統(tǒng)中細(xì)胞通訊的杰出模式。了解酶催化磷酸酯水解的細(xì)節(jié)可能會(huì)擴(kuò)展我們對(duì)酶如何催化化學(xué)反應(yīng)的一般理解。許多磷酸酶抑制劑具有模仿天然磷酸化底物的電荷和幾何形狀的功能。最直接的取代是用不可水解的膦酸酯代替磷酸酯部分。這些衍生物及其類似物通常是金屬磷酸酶的弱抑制劑。帶有側(cè)基配體的膦酸被證明是有效的金屬磷酸酶抑制劑。結(jié)合抑制劑的結(jié)構(gòu)活性研究，使用X射線結(jié)構(gòu)分析來說明兩種抑制劑與堿性磷酸酶的各種結(jié)合方式。蛋白質(zhì)-蛋白質(zhì)相互作用控制著許多生物學(xué)過程。本文描述了位點(diǎn)特異性蛋白質(zhì)修飾工具的合成。該工具可用于探討這些相互作用對(duì)蛋白質(zhì)酪氨酸磷酸酶（PTPase）活性和/或抑制的重要性。這些分子被設(shè)計(jì)為易于將PTPase特異性抑制劑基序整合到折疊的蛋白質(zhì)框架中。現(xiàn)在，這種展示出來的抑制劑可以“借用”周圍的表面區(qū)域，以增強(qiáng)PTPase的識(shí)別能力。所描述的合成提供了有效調(diào)節(jié)特定蛋白-抑制劑結(jié)合物的組合方法。基于酶反應(yīng)機(jī)理開發(fā)人工催化劑的歷史悠久。這些努力中的許多在很大程度上都沒有成功。硫酸酯酶利用的催化機(jī)制被連接到環(huán)糊精支架上。研究了該仿生模型作為酯水解的催化劑。另外，簡單的醛水合物被測定為水解催化劑?？偟膩碚f，這些化學(xué)方法旨在增進(jìn)我們對(duì)酶催化作用的理解。

著錄項(xiàng)

  • 作者

    Antonelli, Stephen Michael.;

  • 作者單位

    Indiana University.;

  • 授予單位 Indiana University.;
  • 學(xué)科 Chemistry Organic.
  • 學(xué)位 Ph.D.
  • 年度 2001
  • 頁碼 156 p.
  • 總頁數(shù) 156
  • 原文格式 PDF
  • 正文語種 eng
  • 中圖分類 有機(jī)化學(xué);
  • 關(guān)鍵詞

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