Aptamers from cell-based selection for bioanalytical applications.
Aptamers from cell-based selection for bioanalytical applications.
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DOI:
10.1021/cr300468w
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发表时间:
2013-04-10
期刊:
影响因子:
62.1
通讯作者:
Jiang J
中科院分区:
文献类型:
--
作者:
Tan W;Donovan MJ;Jiang J
Nucleic acids are the foundation of life. Specific sequences translate certain genetic traits, protein expression, and, ultimately, cellular function. Yet, nucleic acids not only store genetic information, but they can be very useful for the recognition of biological compounds. These molecules, when in single-stranded form, are called aptamers, which have gained much attention by harnessing the ability of nucleic acids to target certain biological molecules. More specifically, aptamers have the potential to be a very effective tool in bioanalysis. As the applications for aptamers evolve and the bioavailability of aptamers improves, the realization of their usefulness is increasing. Aptamers can be derived from a process termed “systematic evolution of ligands by exponential enrichment”(SELEX). To develop aptamers for cell membrane targets, a process termed cell-SELEX is used. The development of aptamers for applications has greatly expanded since their inception approximately two decades ago. Many of these developments, particularly those for biomedical applications, are still at the research stage, but results are promising. One promising area is biomarker discovery. Much effort has been put into biomarker discovery, but improvement is still needed. Proteomic methods, such as two-dimensional gel electrophoresis (2D-GE) and differential imaging gel electrophoresis (DIGE), followed by mass spectrometry (MS) identification of proteins, have been employed for biomarker discovery, but with limited results. The elucidation of membrane proteins that are differentially expressed in disease is still a challenge. 1, 2 Furthermore, both MS and 2D-GE fail to give a full representation of cellular membrane proteins. MS serves as an effective tool for analytical purposes. However, its sensitivity is limited to the nanomolar range for protein concentrations, thus hindering its ability to detect a large
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