蛋白质多维色谱分离与荧光标记定量新方法研究
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摘要
蛋白质基础研究将在分子、细胞和生物体等多个层次上全面揭示生命现象的本质,是后基因组时代的主要研究任务。蛋白质科学研究成果将催生一系列新的技术发展,全面改善人类的生活健康和医疗水平,并引领未来生命科学发展。目前对已经鉴定的人体蛋白质中尚缺乏关键的浓度含量信息,这将对生物标志物蛋白的发现、蛋白功能验证等研究问题造成了巨大困难。因此需要研究新的分离鉴定技术方法对已经鉴定的蛋白进行准确定量。论文围绕蛋白质组分离与定量开展了新技术新方法的研究。以多维色谱分离定量技术与荧光标记技术作为基础,探索了基十荧光标记与色谱分离的蛋白质定量新技术。在OPA、IAF荧光标记蛋白定量方面取得了突破,同时探索了末端肽段标记定量新方法。
第一章对蛋白质分离、鉴定与定量技术进行了综述,主要包括色谱、质谱在蛋白质研究中的作用以及多维液相色谱系统在蛋白质与肽段分离中的应用。
第二章建立了蛋白质样品酶解、在线捕集技术。首先对蛋白质的快速酶解反应器进行了探索。使用固定化酶的功能磁球作为蛋白质酶解的载体,结合芯片反应器微通道的优势,使得低浓度蛋白质的快速酶解得以实现。最低有效酶解蛋白质的浓度为5ng/μl。芯片酶解反应器的开发为蛋白质经多维液相分离后的快速酶解鉴定打下基础。随后对在线捕集分离系统进行定量评估,将整体柱应用于样品的在线捕集与除盐,使用MALDI对抗生素进行检测。使用石墨烯与氧化石墨烯作为MALDI检测的基质与富集材料。通过定量研究待测样品的各种信息,建立起可靠的在线捕集分离与检测系统。
第三章建立了蛋白质快速荧光衍生与色谱定量新技术。基于在线捕集分离系统的研究成果,通过蛋白质快速荧光衍生,将多维液相系统应用于蛋白质定量的研究工作。使用OPA衍生方法作为蛋白质荧光标记的基准反应。同时比较了溶液衍生与固相衍生的结果,将在线固相衍牛技术应用于蛋白质荧光标记反应中。使用在线固相衍生反应,对蛋白质进行快速荧光标记,标记时间在1分钟内完成。通过固相衍生,成功对低浓度蛋白质(5ng/uL)进行荧光标记。由于OPA试剂没有本底荧光信号,因此可以避免除去多余反应原料的操作步骤,减少样品的损失。使用优化的蛋白质OPA固相衍生的反应条件,对人肝中的部分蛋白进行衍生并使用多维液相系统分离蛋白质,得到相应的荧光色谱数据。
第四章建立了基于色谱定量与质谱定性联合工作原理的蛋白质绝对定量技术。基于多维液相系统用于蛋白质定量研究的工作基础,进一步使用质谱分析对目标蛋白进行定性。使用荧光标记的标准合成肽段作为内标,对蛋白质进行绝对定量。选择标记于蛋白质半胱氨酸位点的荧光标记试剂(IAF)。荧光标记试剂的选择原则包括：荧光量子产率、MALDI质谱鉴定的兼容性。荧光标记试剂IAF在质谱串级谱图中不产生碎片离子,对蛋白质搜库后的鉴定结果不产生干扰。将荧光探针IAF标记于蛋白质的半胱氨酸位点,使用二维液相色谱进行蛋白质分离定量、激光诱导荧光技术进行检测。标准蛋白最低定量检测限为0.34amol。通过优化二维色谱的色谱柱组合、色谱条件,对人肝部分蛋白组样品进行了绝对定量。同时对正常人的尿样蛋白组样品进行了全谱的绝对定量。
第五章建立了蛋白质N末端肽段的定量工作。从现有的蛋白质组学技术角度考虑,肽段的色谱分离技术相对成熟,因此基于肽段色谱分离技术的蛋白质定量新方法有一定的可行性。有研究表明,蛋白质末端肽段的序列对于确定蛋白质种类具有唯一性。首先研究了区分蛋白质N末端肽段与非末端肽段的化学衍生与纯化方法。使用小分子对蛋白质分子中裸露的氨基进行封闭反应,随后使用三氟甲磺酸基官能团材料纯化N末端肽段。在获得稳定末端肽段的基础上,荧光探针分子定量标记。最后使用液相色谱分离定量末端肽段,使用激光诱导荧光检测器对末端肽段进行检测。
Biology in general and systems biology in particular increasingly requires the detection and quantification of large numbers of analytes. Since only the quantity of proteins can reflect the status and changes of a biological system, quantitative proteomic nowadays plays an important role in the comparison of biological systems. For the past decades, different techniques for this purpose have been developed. In this study, we focused on developing novel quantitative proteomics strategies based on multi-dimensional liquid chromatography, inventing OPA and IAF fluorescent labeling method for proteins quantification and establishing a new protein quantification strategy based on N-terminal peptide.
In chapter1, the recent developments of the separation and identification techniques for proteomics analysis were reviewed. The requirements and current techniques for multi-dimensional liquid chromatography separation were introduced. The research background was demonstrated.
In chapter2, an easily replaceable microchip enzymatic micro reactor has been fabricated based on the glass microchip with trypsin-immobilized superparamagnetic nanoparticles. Amine-functionalized magnetic nanoparticles with trypsin immobilized were packed onto the glass microchip by the application of a strong magnetic field. Complete protein digestion was achieved in a short time (10s) under the flow rate of5μL/min. These results are expected to open up a new possibility for the proteolysis analysis as well as a new application of magnetic nanoparticles. It takes less than1min under the condition of extra magnetic to form a new packing bed. This micro reactor was also successfully applied to the analysis of an RPLC fraction of the rat liver extract. Besides, an on-line sample enrichment system was evaluated and applied to trace-level bio-molecules quantification using monolithic trapping columns in capillary liquid chromatography (LC) system. The monolithic trapping column is used in front of the analytical column to increase sensitivity, enhance sample loading amount and minimize the loading time. Online trapping system has the advantages of easy handling and labor saving by the column switch system. Results demonstrated high efficiency of the monolithic trapping columns for trapping analytes in online capillary LC system.
In chapter3, a simple OPA method of solid-support labeling for picomoles of proteins in diluted solution was developed. A C18cartridge was used for proteins capture and subsequent labeling with OPA. The use of the solid-support reactor allows easy handling for protein enrichment and purification. The employed OPA reagents for protein assay give no self-fluorescence. The application of OPA labeling method leaved no potential interferences for the assay and extra separation step of the proteins from interferences. Using Casein as a test protein, we have labeled and detected5ng/uL casein. This method was applied to analyze the fraction from weak anion-exchange chromatography (WAX) of human liver extract.
In chapter4, a facile proteomic quantification method, fluorescent labeling absolute quantification (FLAQ), was developed. Instead of using mass spectrometry (MS) for quantification, the FLAQ method is a chromatography-based quantification in combining with MS for identification. Multi-dimensional liquid chromatography (MDLC) with laser-induced fluorescence (LIF) detection with high accuracy and tandem MS system were employed for FLAQ. A fluorescence dye,5-iodoacetamidofluorescein, was finally chosen to label proteins on all cysteine residues. The fluorescent dye was compatible with the process of the trypsin digestion and MALD1MS identification. The limit of quantitation for the model protein was as low as0.34amol. Parts of proteins in human liver proteome were quantified and demonstrated using FLAQ.
In chapter5, a new strategy for protein quantification was studied based on N-terminal peptide of proteins. In detail.(1) Based on N-peptide isolation, quantification information of proteins can be obtained by HPLC separation.(2) Using the functional materials and amino group blocking reactions, the terminal peptides were successfully separated and isolated.(3) Qualification and identification of proteins by the technology of N-terminal peptide location. By the new technology, protein can be quantified with high accuracy and reliability. By the development of novel technology for protein quantification, we are promising to supply the techniques for the protein science to find potential functional proteins and biomarker.
第一章对蛋白质分离、鉴定与定量技术进行了综述,主要包括色谱、质谱在蛋白质研究中的作用以及多维液相色谱系统在蛋白质与肽段分离中的应用。
第二章建立了蛋白质样品酶解、在线捕集技术。首先对蛋白质的快速酶解反应器进行了探索。使用固定化酶的功能磁球作为蛋白质酶解的载体,结合芯片反应器微通道的优势,使得低浓度蛋白质的快速酶解得以实现。最低有效酶解蛋白质的浓度为5ng/μl。芯片酶解反应器的开发为蛋白质经多维液相分离后的快速酶解鉴定打下基础。随后对在线捕集分离系统进行定量评估,将整体柱应用于样品的在线捕集与除盐,使用MALDI对抗生素进行检测。使用石墨烯与氧化石墨烯作为MALDI检测的基质与富集材料。通过定量研究待测样品的各种信息,建立起可靠的在线捕集分离与检测系统。
第三章建立了蛋白质快速荧光衍生与色谱定量新技术。基于在线捕集分离系统的研究成果,通过蛋白质快速荧光衍生,将多维液相系统应用于蛋白质定量的研究工作。使用OPA衍生方法作为蛋白质荧光标记的基准反应。同时比较了溶液衍生与固相衍生的结果,将在线固相衍牛技术应用于蛋白质荧光标记反应中。使用在线固相衍生反应,对蛋白质进行快速荧光标记,标记时间在1分钟内完成。通过固相衍生,成功对低浓度蛋白质(5ng/uL)进行荧光标记。由于OPA试剂没有本底荧光信号,因此可以避免除去多余反应原料的操作步骤,减少样品的损失。使用优化的蛋白质OPA固相衍生的反应条件,对人肝中的部分蛋白进行衍生并使用多维液相系统分离蛋白质,得到相应的荧光色谱数据。
第四章建立了基于色谱定量与质谱定性联合工作原理的蛋白质绝对定量技术。基于多维液相系统用于蛋白质定量研究的工作基础,进一步使用质谱分析对目标蛋白进行定性。使用荧光标记的标准合成肽段作为内标,对蛋白质进行绝对定量。选择标记于蛋白质半胱氨酸位点的荧光标记试剂(IAF)。荧光标记试剂的选择原则包括：荧光量子产率、MALDI质谱鉴定的兼容性。荧光标记试剂IAF在质谱串级谱图中不产生碎片离子,对蛋白质搜库后的鉴定结果不产生干扰。将荧光探针IAF标记于蛋白质的半胱氨酸位点,使用二维液相色谱进行蛋白质分离定量、激光诱导荧光技术进行检测。标准蛋白最低定量检测限为0.34amol。通过优化二维色谱的色谱柱组合、色谱条件,对人肝部分蛋白组样品进行了绝对定量。同时对正常人的尿样蛋白组样品进行了全谱的绝对定量。
第五章建立了蛋白质N末端肽段的定量工作。从现有的蛋白质组学技术角度考虑,肽段的色谱分离技术相对成熟,因此基于肽段色谱分离技术的蛋白质定量新方法有一定的可行性。有研究表明,蛋白质末端肽段的序列对于确定蛋白质种类具有唯一性。首先研究了区分蛋白质N末端肽段与非末端肽段的化学衍生与纯化方法。使用小分子对蛋白质分子中裸露的氨基进行封闭反应,随后使用三氟甲磺酸基官能团材料纯化N末端肽段。在获得稳定末端肽段的基础上,荧光探针分子定量标记。最后使用液相色谱分离定量末端肽段,使用激光诱导荧光检测器对末端肽段进行检测。
Biology in general and systems biology in particular increasingly requires the detection and quantification of large numbers of analytes. Since only the quantity of proteins can reflect the status and changes of a biological system, quantitative proteomic nowadays plays an important role in the comparison of biological systems. For the past decades, different techniques for this purpose have been developed. In this study, we focused on developing novel quantitative proteomics strategies based on multi-dimensional liquid chromatography, inventing OPA and IAF fluorescent labeling method for proteins quantification and establishing a new protein quantification strategy based on N-terminal peptide.
In chapter1, the recent developments of the separation and identification techniques for proteomics analysis were reviewed. The requirements and current techniques for multi-dimensional liquid chromatography separation were introduced. The research background was demonstrated.
In chapter2, an easily replaceable microchip enzymatic micro reactor has been fabricated based on the glass microchip with trypsin-immobilized superparamagnetic nanoparticles. Amine-functionalized magnetic nanoparticles with trypsin immobilized were packed onto the glass microchip by the application of a strong magnetic field. Complete protein digestion was achieved in a short time (10s) under the flow rate of5μL/min. These results are expected to open up a new possibility for the proteolysis analysis as well as a new application of magnetic nanoparticles. It takes less than1min under the condition of extra magnetic to form a new packing bed. This micro reactor was also successfully applied to the analysis of an RPLC fraction of the rat liver extract. Besides, an on-line sample enrichment system was evaluated and applied to trace-level bio-molecules quantification using monolithic trapping columns in capillary liquid chromatography (LC) system. The monolithic trapping column is used in front of the analytical column to increase sensitivity, enhance sample loading amount and minimize the loading time. Online trapping system has the advantages of easy handling and labor saving by the column switch system. Results demonstrated high efficiency of the monolithic trapping columns for trapping analytes in online capillary LC system.
In chapter3, a simple OPA method of solid-support labeling for picomoles of proteins in diluted solution was developed. A C18cartridge was used for proteins capture and subsequent labeling with OPA. The use of the solid-support reactor allows easy handling for protein enrichment and purification. The employed OPA reagents for protein assay give no self-fluorescence. The application of OPA labeling method leaved no potential interferences for the assay and extra separation step of the proteins from interferences. Using Casein as a test protein, we have labeled and detected5ng/uL casein. This method was applied to analyze the fraction from weak anion-exchange chromatography (WAX) of human liver extract.
In chapter4, a facile proteomic quantification method, fluorescent labeling absolute quantification (FLAQ), was developed. Instead of using mass spectrometry (MS) for quantification, the FLAQ method is a chromatography-based quantification in combining with MS for identification. Multi-dimensional liquid chromatography (MDLC) with laser-induced fluorescence (LIF) detection with high accuracy and tandem MS system were employed for FLAQ. A fluorescence dye,5-iodoacetamidofluorescein, was finally chosen to label proteins on all cysteine residues. The fluorescent dye was compatible with the process of the trypsin digestion and MALD1MS identification. The limit of quantitation for the model protein was as low as0.34amol. Parts of proteins in human liver proteome were quantified and demonstrated using FLAQ.
In chapter5, a new strategy for protein quantification was studied based on N-terminal peptide of proteins. In detail.(1) Based on N-peptide isolation, quantification information of proteins can be obtained by HPLC separation.(2) Using the functional materials and amino group blocking reactions, the terminal peptides were successfully separated and isolated.(3) Qualification and identification of proteins by the technology of N-terminal peptide location. By the new technology, protein can be quantified with high accuracy and reliability. By the development of novel technology for protein quantification, we are promising to supply the techniques for the protein science to find potential functional proteins and biomarker.
引文
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