Bioorthogonal chemistry:a covalent strategy for the study of biological systems  被引量:2

Bioorthogonal chemistry:a covalent strategy for the study of biological systems

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作  者:LIM Reyna K.V. 

机构地区:[1]Department of Chemistry,State University of New York at Buffalo

出  处:《Science China Chemistry》2010年第1期61-70,共10页中国科学(化学英文版)

基  金:supported by the US National Institutes of Health (R01 GM085092) and New York State Center of Excellence in Bioinformatics and Life Sciences

摘  要:The development of genetically encoded,wavelength-tunable fluorescent proteins has provided a powerful imaging tool to the study of protein dynamics and functions in cellular and organismal biology.However,many biological functions are not directly encoded in the protein primary sequence,e.g.,dynamic regulation afforded by protein posttranslational modifications such as phosphorylation.To meet this challenge,an emerging field of bioorthogonal chemistry has promised to offer a versatile strategy to selectively label a biomolecule of interest and track their dynamic regulations in its native habitat.This strategy has been successfully applied to the studies of all classes of biomolecules in living systems,including proteins,nucleic acids,carbohydrates,and lipids.Whereas the incorporation of a bioorthogonal reporter site-selectively into a biomolecule through either genetic or metabolic approaches has been well established,the development of bioorthogonal reactions that allow fast ligation of exogenous chemical probes with the bioorthogonal reporter in living systems remains in its early stage.Here,we review the recent development of bioorthogonal reactions and their applications in various biological systems,with a detailed discussion about our own work―the development of the tetrazole-based,photoinducible 1,3-dipolar cycloaddition reaction.The development of genetically encoded,wavelength-tunable fluorescent proteins has provided a powerful imaging tool to the study of protein dynamics and functions in cellular and organismal biology.However,many biological functions are not directly encoded in the protein primary sequence,e.g.,dynamic regulation afforded by protein posttranslational modifications such as phosphorylation.To meet this challenge,an emerging field of bioorthogonal chemistry has promised to offer a versatile strategy to selectively label a biomolecule of interest and track their dynamic regulations in its native habitat.This strategy has been successfully applied to the studies of all classes of biomolecules in living systems,including proteins,nucleic acids,carbohydrates,and lipids.Whereas the incorporation of a bioorthogonal reporter site-selectively into a biomolecule through either genetic or metabolic approaches has been well established,the development of bioorthogonal reactions that allow fast ligation of exogenous chemical probes with the bioorthogonal reporter in living systems remains in its early stage.Here,we review the recent development of bioorthogonal reactions and their applications in various biological systems,with a detailed discussion about our own work―the development of the tetrazole-based,photoinducible 1,3-dipolar cycloaddition reaction.

关 键 词:bioorthogonal reaction proteins biotechnology 1 3-dipolar CYCLOADDITION CLICK CHEMISTRY TETRAZOLE 

分 类 号:Q50[生物学—生物化学]

 

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