DICP OpenIR
Subject Area分析化学
Protein imprinted materials for Proteomic Study
Zhang LH(张丽华); Zhang YK(张玉奎)
Source PublicationDICP Symposium (XXIX) onInternational Forum on Molecular Imprinting (2011)
Conference NameDICP Symposium (XXIX) onInternational Forum on Molecular Imprinting (2011)
Conference Date2011-10-5
2011
Conference Place大连
Pages33-0
Publisher待补充
Publication Place待补充
Cooperation Status特邀报告
Department1810
Funding Organization大连化学物理研究所
AbstractWith the recent development of proteome techniques, the interest in finding biomarkers from human plasma for clinical diagnosis has gained new momentum. However, the wide dynamic range of proteins in abundance, over 1010, brings great challenges to discover low abundance proteins with significant biological functions. [1] Therefore, in proteome study, it is indispensable to deplete high abundance proteins to identify low abundance ones. Antibody techniques have been proven the most effective methods. [1] However, with the consideration of stability, robustness and cost, the development of artificial antibody, molecularly imprinted materials, might be a state-of-the-art solution. Three generations of protein imprinted materials were developed in our study for proteomics application. In the first generation, macroporous protein-imprinted monolithic polyacrylamide materials was prepared by 3-D imprinting strategy and applied to extract the target proteins from complex protein mixtures by affinity chromatography[2]. In the second generation, one new approach, combining metal-coordination with surface imprinting technology, was developed to prepare protein-affinity materials, which showed higher specific recognition ability towards the target proteins[3]. The other new approach in the second generation, hierarchical imprinting, was developed and applied for high abundance protein imprinting. In the third generation, the epitope of the target protein was applied to overcome the difficulty in obtaining the pure protein as the template. Meanwhile, environmental-friendly polymer self-assembly technology, instead of polymerization, was applied to fabricate the materials.; With the recent development of proteome techniques, the interest in finding biomarkers from human plasma for clinical diagnosis has gained new momentum. However, the wide dynamic range of proteins in abundance, over 1010, brings great challenges to discover low abundance proteins with significant biological functions. [1] Therefore, in proteome study, it is indispensable to deplete high abundance proteins to identify low abundance ones. Antibody techniques have been proven the most effective methods. [1] However, with the consideration of stability, robustness and cost, the development of artificial antibody, molecularly imprinted materials, might be a state-of-the-art solution. Three generations of protein imprinted materials were developed in our study for proteomics application. In the first generation, macroporous protein-imprinted monolithic polyacrylamide materials was prepared by 3-D imprinting strategy and applied to extract the target proteins from complex protein mixtures by affinity chromatography[2]. In the second generation, one new approach, combining metal-coordination with surface imprinting technology, was developed to prepare protein-affinity materials, which showed higher specific recognition ability towards the target proteins[3]. The other new approach in the second generation, hierarchical imprinting, was developed and applied for high abundance protein imprinting. In the third generation, the epitope of the target protein was applied to overcome the difficulty in obtaining the pure protein as the template. Meanwhile, environmental-friendly polymer self-assembly technology, instead of polymerization, was applied to fabricate the materials.
Language英语
Document Type会议论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/116017
Collection中国科学院大连化学物理研究所
Corresponding AuthorZhang YK(张玉奎)
Recommended Citation
GB/T 7714
Zhang LH,Zhang YK. Protein imprinted materials for Proteomic Study[C]. 待补充:待补充,2011:33-0.
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