环糊精谷胱甘肽过氧化物酶模拟物的构建、催化机制及其生物学活性研究
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摘要
谷胱甘肽过氧化物酶（GPX）属于硒蛋白家族，是生物体内重要的抗氧化酶之一，它可以消除体内的过氧化氢、脂质过氧化物等活性氧（ROS）物质，对于防治ROS引起的疾病，如动脉粥样硬化、辐射损伤、克山病和心血管疾病等有着巨大的药用价值。但长期以来，由于天然GPX存在不稳定（酶水解以及半衰期短）、来源有限、异源表达困难等诸多方面的缺陷，使得它的开发利用受到极大的限制。因而，对GPX的模拟以及开发治疗相关疾病的药物一直为国内外科学家所关注。
我们从酶催化的本质(底物的识别、结合以及分子内催化)出发，利用超分子化学的原理与方法，选择主体分子——环糊精作为结合底物客体分子的骨架分子，构建了环糊精GPX模型体系。主要开展了以下工作：
1.设计合成了三种具有GPX活性的2位碲桥联环糊精
为了探究尺寸匹配效应对环糊精GPX模拟酶催化过程的重要性，我们选择以三种母体环糊精为模板，通过化学修饰在环糊精的次面引入催化基团碲构建了含碲环糊精GPX模型体系，并用三种不同结构的氢过氧化物，即过氧化氢(H_2O_2)，叔丁基过氧化氢(t-BuOOH)和枯烯过氧化氢(CuOOH)，考察含碲环糊精GPX模型体系的催化活性。研究结果发现：2位碲桥联γ-环糊精（2-Te-γ-CD）的催化活性最高，其催化GSH还原H_2O_2，t-BuOOH和CuOOH的活力分别是传统“小分子硒酶”Ebselen的80.5，333.3和118.3倍；含碲环糊精GPX模型体系对过氧化氢底物存在底物特异性，其中对CuOOH的结合最强，而对H_2O_2最差；通过考察三种模拟物催化GSH还原氢过氧化物反应的动力学，发现反应初速度对底物浓度的双倒数曲线为一组平行线，均表现出了米氏动力学特征，表明三种GPX模拟物以GSH为底物催化氢过氧化物的机理可能为乒乓机制，与天然酶的催化机理相似。
2.研究了GPX模型2-Te-γ-CD的底物识别与催化机理
首先利用UV-vis吸收光谱研究了GPX的2-Te-γ-CD与底物GSH的一个带有生色团的替代物——GSH-S-DNP相互作用的分子机制，结果表明2-Te-γ-CD能GSH-S-DNP形成化学计量比为1：1的复合物。其次，利用1H NMR技术研究了2-Te-γ-CD与底物GSH的相互作用机理。研究结果表明GSH与2-Te-γ-CD形成了化学计量比为1：2的复合物；(2-Te-γ-CD)_2/GSH的复合常数显示它们的复合能力属于中等强度，正是这些中等强度复合中间体的存在大大地提高了2-Te-γ-CD的GPX活性，这一研究揭示了2-Te-γ-CD拥有较高GPX活性的本质机理。再者，利用电喷雾质谱（ESI-MS）及串联质谱技术（ESI-MS/MS），在线监控了2-TeCD催化GSH还原H_2O_2的反应过程。通过将微型反应器与ESI离子源直接相连，实现了在极短时间内对反应体系中间体的快速筛选，利用该技术成功地捕获了2-TeCD催化反应过程中的三个关键性中间体，并对其结构进行了详细的分析。研究结果表明，2-TeCD是通过碲醇、次碲酸、碲硫化物来展现其GPX活性，与天然GPX的催化机制类似。
3.构建了基于γ-环糊精的GPX模型体系
利用化学手段合成了7种基于γ-环糊精的GPx模拟物，采用元素分析、红外光谱、13CNMR和1H NMR等对它们的结构进行了详细表征。GPX活性研究表明6,6’双碲桥联γ-环糊精（6-diTe-γ-CD）的GPX活性最高，其催化GSH还原H_2O_2，t-BuOOH和CuOOH的活力分别是Ebselen的147.3，1897.9和663.9倍。对6-diTe-γ-CD的稳态动力学研究表明，其催化机制为乒乓机制，与天然酶遵循相同的催化机理。催化过程中双底物GSH和ROOH对6-diTe-γ-CD有竞争性亲和结合作用。
4.开展了环糊精GPX模拟物保护线粒体抗氧化损伤研究
线粒体是体内ROS产生的主要场所，因而我们建立了线粒体的Fe2+/Vc诱导损伤体系来研究GPX模拟物的生物学效应。研究结果证明了受氧化损伤后的线粒体发生如下变化：膨胀度异常增大、脂质过氧化产物——丙二醛（MDA）大量生成、细胞色素氧化酶活性下降。环糊精GPX模拟酶能不同程度的降低MDA的生成、抑制线粒体的膨胀，抑制细胞色素氧化酶活性的下降。其中，6-diTe-γ-CD和2-Te-γ-CD保护线粒体免遭ROS损伤的能力强于其他GPX模拟酶及传统小分子硒酶“Ebselen”，因此有望成为治疗心血管疾病的新药前体化合物。
Glutathione peroxidase is an important mammalian selenoenzyme that function in cellularredox reactions and plays an essential role in the detoxification of hydroperoxides in vivo, therebyscavenging active oxygen, protecting biomembranes from oxidative stress. It is related to manydiseases and it is regarded as one of the most important antioxidant enzymes in living organisms.However, native GPx has some shortcomings, such as instability, antigenicity and pooravailability, which have limited its therapeutic use. In addition, it is extremely difficult tosynthesize selenium-containing proteins by traditional recombinant DNA methods; thereforeconsiderable effort has been spent to find other routes to compounds capable of imitating theproperties of GPx.
On the basis of structure and catalytic mechanism understanding for GPX, we choosecyclodextrins as the scaffolds of enzyme models to establish the systems of GPX models based oncyclodextrin.
1. Cyclodextrin-Derived Chalcogenides as Glutathione Peroxidase Mimics
To elucidate the importance of the goodness of fit in complexes between substrates andglutathione peroxidise (GPX) mimics, we examined the decomposition of a variety of structurallydistinct hydroperoxides at the expense of glutathione (GSH) catalyzed by2,2’-ditellurobis(2-deoxy-γ-cyclodextrin)(2-Te-γ-CD) and by the corresponding derivatives ofβ-cyclodextrin (β-CD) and α-cyclodextrin. Hydroperoxides decomposing capacity of2-Te-γ-CDwas determined to be80.5,109.8,149.6U/μmol, respectively, with H_2O_2, t-BuOOH and CuOOH,which was almost80.5,333.3,118.3-fold than that of Ebselen. Furthermore, the catalytic constantand the combination with the best binding also exhibited the highest regioselectivity in thesubstrate decomposition. Saturation kinetics was observed and the catalytic reaction agreed with aping-pong mechanism, in analogy with natural GPX.
2. Studies on the Molecular Recognition and Related Catalytic Mechanism of BridgedBis-cyclodextrins
As the substitutes of glutathione (GSH), S-substituted dinitrophenyl glutathione(GSH-S-DNP) are used in the present study to explore the recognition mechanism between twoglutathione peroxidase (GPX) mimics and GSH. The effect of the addition of γ-CD, or2-Te-γ-CDto the phosphate buffer solutions of GSH-S-DNP has been fully investigated by means ofUltraviolet-visible (UV-vis) absorption. The stoichiometry of the inclusion complex wasdetermined to be of2:1host-to-guest. The value of stability constant Kcfor (2-Te-γ-CD)_2/GSH atroom temperature was calculated to be3.815×104M-2, which suggested that2-Te-γ-CD had amoderate ability to bind GSH. Importantly, the proposed mode of the (2-TeCD)2/GSH complexwas the possible important noncovalent interactions between enzymes and substrates ininfluencing catalysis and binding. Using electrospray ionization mass (and tandem) spectrometry(ESI-MS and ESI-MS/MS) spectrometric experiments, the decomposition of hydrogen peroxide atthe expense of GSH catalyzed by2-TeCD was monitored on-line. The key intermediates weresuccessfully intercepted and structurally characterized for the first time by coupling a microreactoron-line to the ESI ion source, which permitted the fast screening of intermediates directly fromsolution. The catalytic mechanism of2-TeCD catalysis has been elaborated based on massspectrometric data and exerted its peroxidase activity via tellurol, tellurenic acid, andtellurosulfide, in analogy with natural GPX.
3. Gamma-Cyclodextrin-Derived Chalcogenides as Glutathione Peroxidase Mimics
A series of novel glutathione peroxidase (GPx) mimics based on organochalcogencyclodextrin dimer were synthesized. Their GPx-like antioxidant activities were studied usingH_2O_2, t-BuOOH, and CuOOH as substrates and glutathione as thiol co-substrate. The resultsshowed that6A,6B-ditelluronic acid-A’,6B’-tellurium bridged γ-cyclodextrin (6-diTe-γ-CD) hadthe highest peroxidase activity, which was approximately670-fold higher than Ebselen, awell-known GPx mimic. Reduction of lipophilic CuOOH often proceeded much faster thanreduction of the more hydrophilic H_2O_2or t-BuOOH, which cannot bind into the hydrophobicinterior of the cyclodextrin. Saturation kinetics was observed and the catalytic reaction agreedwith a ping-pong mechanism, in analogy with natural GPX.
4. Cyclodextrin Derivatives as Glutathione Peroxidase Mimics and Their Protection ofMitochondria against Oxidative Damage
The biological activities were also evaluated for their capacity to protect mitochondriaagainst Ferrous sulfate/ascorbate-induced oxidative damage.6-diTe-γ-CD was the best inhibitor which significantly suppressed Ferrous sulfate/ascorbate-induced cytotoxicity as determined byswelling of mitochondria, lipid peroxidation and cytochrome c oxidase activity. Our data suggeststhat6-diTe-γ-CD and2-Te-γ-CD has potential pharmaceutical application in the treatment ofROS-mediated diseases.
我们从酶催化的本质(底物的识别、结合以及分子内催化)出发，利用超分子化学的原理与方法，选择主体分子——环糊精作为结合底物客体分子的骨架分子，构建了环糊精GPX模型体系。主要开展了以下工作：
1.设计合成了三种具有GPX活性的2位碲桥联环糊精
为了探究尺寸匹配效应对环糊精GPX模拟酶催化过程的重要性，我们选择以三种母体环糊精为模板，通过化学修饰在环糊精的次面引入催化基团碲构建了含碲环糊精GPX模型体系，并用三种不同结构的氢过氧化物，即过氧化氢(H_2O_2)，叔丁基过氧化氢(t-BuOOH)和枯烯过氧化氢(CuOOH)，考察含碲环糊精GPX模型体系的催化活性。研究结果发现：2位碲桥联γ-环糊精（2-Te-γ-CD）的催化活性最高，其催化GSH还原H_2O_2，t-BuOOH和CuOOH的活力分别是传统“小分子硒酶”Ebselen的80.5，333.3和118.3倍；含碲环糊精GPX模型体系对过氧化氢底物存在底物特异性，其中对CuOOH的结合最强，而对H_2O_2最差；通过考察三种模拟物催化GSH还原氢过氧化物反应的动力学，发现反应初速度对底物浓度的双倒数曲线为一组平行线，均表现出了米氏动力学特征，表明三种GPX模拟物以GSH为底物催化氢过氧化物的机理可能为乒乓机制，与天然酶的催化机理相似。
2.研究了GPX模型2-Te-γ-CD的底物识别与催化机理
首先利用UV-vis吸收光谱研究了GPX的2-Te-γ-CD与底物GSH的一个带有生色团的替代物——GSH-S-DNP相互作用的分子机制，结果表明2-Te-γ-CD能GSH-S-DNP形成化学计量比为1：1的复合物。其次，利用1H NMR技术研究了2-Te-γ-CD与底物GSH的相互作用机理。研究结果表明GSH与2-Te-γ-CD形成了化学计量比为1：2的复合物；(2-Te-γ-CD)_2/GSH的复合常数显示它们的复合能力属于中等强度，正是这些中等强度复合中间体的存在大大地提高了2-Te-γ-CD的GPX活性，这一研究揭示了2-Te-γ-CD拥有较高GPX活性的本质机理。再者，利用电喷雾质谱（ESI-MS）及串联质谱技术（ESI-MS/MS），在线监控了2-TeCD催化GSH还原H_2O_2的反应过程。通过将微型反应器与ESI离子源直接相连，实现了在极短时间内对反应体系中间体的快速筛选，利用该技术成功地捕获了2-TeCD催化反应过程中的三个关键性中间体，并对其结构进行了详细的分析。研究结果表明，2-TeCD是通过碲醇、次碲酸、碲硫化物来展现其GPX活性，与天然GPX的催化机制类似。
3.构建了基于γ-环糊精的GPX模型体系
利用化学手段合成了7种基于γ-环糊精的GPx模拟物，采用元素分析、红外光谱、13CNMR和1H NMR等对它们的结构进行了详细表征。GPX活性研究表明6,6’双碲桥联γ-环糊精（6-diTe-γ-CD）的GPX活性最高，其催化GSH还原H_2O_2，t-BuOOH和CuOOH的活力分别是Ebselen的147.3，1897.9和663.9倍。对6-diTe-γ-CD的稳态动力学研究表明，其催化机制为乒乓机制，与天然酶遵循相同的催化机理。催化过程中双底物GSH和ROOH对6-diTe-γ-CD有竞争性亲和结合作用。
4.开展了环糊精GPX模拟物保护线粒体抗氧化损伤研究
线粒体是体内ROS产生的主要场所，因而我们建立了线粒体的Fe2+/Vc诱导损伤体系来研究GPX模拟物的生物学效应。研究结果证明了受氧化损伤后的线粒体发生如下变化：膨胀度异常增大、脂质过氧化产物——丙二醛（MDA）大量生成、细胞色素氧化酶活性下降。环糊精GPX模拟酶能不同程度的降低MDA的生成、抑制线粒体的膨胀，抑制细胞色素氧化酶活性的下降。其中，6-diTe-γ-CD和2-Te-γ-CD保护线粒体免遭ROS损伤的能力强于其他GPX模拟酶及传统小分子硒酶“Ebselen”，因此有望成为治疗心血管疾病的新药前体化合物。
Glutathione peroxidase is an important mammalian selenoenzyme that function in cellularredox reactions and plays an essential role in the detoxification of hydroperoxides in vivo, therebyscavenging active oxygen, protecting biomembranes from oxidative stress. It is related to manydiseases and it is regarded as one of the most important antioxidant enzymes in living organisms.However, native GPx has some shortcomings, such as instability, antigenicity and pooravailability, which have limited its therapeutic use. In addition, it is extremely difficult tosynthesize selenium-containing proteins by traditional recombinant DNA methods; thereforeconsiderable effort has been spent to find other routes to compounds capable of imitating theproperties of GPx.
On the basis of structure and catalytic mechanism understanding for GPX, we choosecyclodextrins as the scaffolds of enzyme models to establish the systems of GPX models based oncyclodextrin.
1. Cyclodextrin-Derived Chalcogenides as Glutathione Peroxidase Mimics
To elucidate the importance of the goodness of fit in complexes between substrates andglutathione peroxidise (GPX) mimics, we examined the decomposition of a variety of structurallydistinct hydroperoxides at the expense of glutathione (GSH) catalyzed by2,2’-ditellurobis(2-deoxy-γ-cyclodextrin)(2-Te-γ-CD) and by the corresponding derivatives ofβ-cyclodextrin (β-CD) and α-cyclodextrin. Hydroperoxides decomposing capacity of2-Te-γ-CDwas determined to be80.5,109.8,149.6U/μmol, respectively, with H_2O_2, t-BuOOH and CuOOH,which was almost80.5,333.3,118.3-fold than that of Ebselen. Furthermore, the catalytic constantand the combination with the best binding also exhibited the highest regioselectivity in thesubstrate decomposition. Saturation kinetics was observed and the catalytic reaction agreed with aping-pong mechanism, in analogy with natural GPX.
2. Studies on the Molecular Recognition and Related Catalytic Mechanism of BridgedBis-cyclodextrins
As the substitutes of glutathione (GSH), S-substituted dinitrophenyl glutathione(GSH-S-DNP) are used in the present study to explore the recognition mechanism between twoglutathione peroxidase (GPX) mimics and GSH. The effect of the addition of γ-CD, or2-Te-γ-CDto the phosphate buffer solutions of GSH-S-DNP has been fully investigated by means ofUltraviolet-visible (UV-vis) absorption. The stoichiometry of the inclusion complex wasdetermined to be of2:1host-to-guest. The value of stability constant Kcfor (2-Te-γ-CD)_2/GSH atroom temperature was calculated to be3.815×104M-2, which suggested that2-Te-γ-CD had amoderate ability to bind GSH. Importantly, the proposed mode of the (2-TeCD)2/GSH complexwas the possible important noncovalent interactions between enzymes and substrates ininfluencing catalysis and binding. Using electrospray ionization mass (and tandem) spectrometry(ESI-MS and ESI-MS/MS) spectrometric experiments, the decomposition of hydrogen peroxide atthe expense of GSH catalyzed by2-TeCD was monitored on-line. The key intermediates weresuccessfully intercepted and structurally characterized for the first time by coupling a microreactoron-line to the ESI ion source, which permitted the fast screening of intermediates directly fromsolution. The catalytic mechanism of2-TeCD catalysis has been elaborated based on massspectrometric data and exerted its peroxidase activity via tellurol, tellurenic acid, andtellurosulfide, in analogy with natural GPX.
3. Gamma-Cyclodextrin-Derived Chalcogenides as Glutathione Peroxidase Mimics
A series of novel glutathione peroxidase (GPx) mimics based on organochalcogencyclodextrin dimer were synthesized. Their GPx-like antioxidant activities were studied usingH_2O_2, t-BuOOH, and CuOOH as substrates and glutathione as thiol co-substrate. The resultsshowed that6A,6B-ditelluronic acid-A’,6B’-tellurium bridged γ-cyclodextrin (6-diTe-γ-CD) hadthe highest peroxidase activity, which was approximately670-fold higher than Ebselen, awell-known GPx mimic. Reduction of lipophilic CuOOH often proceeded much faster thanreduction of the more hydrophilic H_2O_2or t-BuOOH, which cannot bind into the hydrophobicinterior of the cyclodextrin. Saturation kinetics was observed and the catalytic reaction agreedwith a ping-pong mechanism, in analogy with natural GPX.
4. Cyclodextrin Derivatives as Glutathione Peroxidase Mimics and Their Protection ofMitochondria against Oxidative Damage
The biological activities were also evaluated for their capacity to protect mitochondriaagainst Ferrous sulfate/ascorbate-induced oxidative damage.6-diTe-γ-CD was the best inhibitor which significantly suppressed Ferrous sulfate/ascorbate-induced cytotoxicity as determined byswelling of mitochondria, lipid peroxidation and cytochrome c oxidase activity. Our data suggeststhat6-diTe-γ-CD and2-Te-γ-CD has potential pharmaceutical application in the treatment ofROS-mediated diseases.
引文
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