Synthesis and Site-Specific Incorporation of Red-Shifted Azobenzene Amino Acids into Proteins.
Synthesis and Site-Specific Incorporation of Red-Shifted Azobenzene Amino Acids into Proteins.
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DOI：
10.1021/acs.orglett.5b03268
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发表时间：
2015-12-18
期刊：
影响因子：
5.2
通讯作者：
Lin Q
中科院分区：
文献类型：
--
作者：
John AA;Ramil CP;Tian Y;Cheng G;Lin Q
通过两步程序以中等至优异的收率合成了一系列红移偶氮苯氨基酸，其中酪氨酸衍生物首先被氧化为相应的醌型螺内酯，然后由硝酸高铈铵催化与取代的苯肼形成偶氮。所得的偶氮苯-丙氨酸衍生物在蓝色（448 nm）或绿色（530 nm）LED 光照射下表现出高效的反式/顺式光转换。此外，通过正交 tRNA/PylRS 对的琥珀密码子抑制，携带偶氮苯-丙氨酸类似物的 9 个超级文件夹绿色荧光蛋白 (sfGFP) 突变体在大肠杆菌中以良好的产量表达，其中一个突变体在 LED 灯下表现出持久的光开关。
A series of red-shifted azobenzene amino acids were synthesized in moderate-to-excellent yields via a two-step procedure in which tyrosine derivatives were first oxidized to the corresponding quinonoidal spirolactones followed by ceric ammonium nitrate-catalyzed azo formation with the substituted phenylhydrazines. The resulting azobenzene–alanine derivatives exhibited efficient trans/cis photoswitching upon irradiation with a blue (448 nm) or green (530 nm) LED light. Moreover, nine superfolder green fluorescent protein (sfGFP) mutants carrying the azobenzene–alanine analogues were expressed in E. coli in good yields via amber codon suppression with an orthogonal tRNA/PylRS pair, and one of the mutants showed durable photoswitching with the LED light.