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Coumarin as a structural component of substrates and probes for serine and cysteine proteases.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics ( IF 2.5 ) Pub Date : 2020-05-13 , DOI: 10.1016/j.bbapap.2020.140445
Julian Breidenbach 1 , Ulrike Bartz 2 , Michael Gütschow 1
Affiliation  

Coumarins represent well-established structures to introduce fluorescence into tool compounds for biochemical investigations. They are valued for their small size, chemical stability and accessibility as well as their tunable photochemical properties. As components of fluorophore/quencher pairs or FRET donor/acceptor pairs, coumarins have frequently been applied in substrate mapping approaches for serine and cysteine proteases. This review also focuses on the incorporation of coumarins into the side chain of amino acids and the exploitation of the resulting fluorescent amino acids for the positional profiling of protease substrates. The protease-inhibiting properties of certain coumarin derivatives and the utilization of coumarin moieties to assemble activity-based probes for serine and cysteine protease are discussed as well.

中文翻译:

香豆素作为丝氨酸和半胱氨酸蛋白酶的底物和探针的结构成分。

香豆素代表了完善的结构,可以将荧光引入用于生化研究的工具化合物中。它们因其体积小,化学稳定性和可及性以及可调节的光化学性质而受到重视。作为荧光基团/猝灭剂对或FRET供体/受体对的成分,香豆素通常用于丝氨酸和半胱氨酸蛋白酶的底物作图方法中。这项审查还侧重于将香豆素掺入氨基酸的侧链,并利用所得的荧光氨基酸对蛋白酶底物进行位置分析。还讨论了某些香豆素衍生物的蛋白酶抑制特性,以及利用香豆素部分组装基于活性的丝氨酸和半胱氨酸蛋白酶的探针。
更新日期:2020-05-13
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