Expanding the fluorous arsenal: tetrafluorinated phenylalanines for protein design.
Expanding the fluorous arsenal: tetrafluorinated phenylalanines for protein design.
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DOI：
10.1021/ja8062309
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发表时间：
2009-01
影响因子：
15
通讯作者：
Hong Zheng;Kristofer Comeforo;Jianmin Gao
中科院分区：
文献类型：
--
作者：
Hong Zheng;Kristofer Comeforo;Jianmin Gao
将四氟化苯丙氨酸整合到绒毛头子结构域 HP35 中，并评估了它们对蛋白质稳定性的能量贡献。与五氟苯丙氨酸相比，含有四氟苯丙氨酸的 HP35 变体表现出大幅提高的热稳定性和热力学稳定性。良好的稳定性归因于高度但不完全氟化的芳环保留并加强了静电 ArH...pi 相互作用。
Tetrafluorinated phenylalanines were incorporated into villin headpiece subdomain HP35, and their energetic contribution to protein stability was evaluated. In comparison to pentafluoro-phenylalanines, HP35 variants harboring tetrafluorinated phenylalanines exhibit increased thermal and thermodynamic stability by a large margin. The favorable stabilization is attributed to the electrostatic ArH...pi interactions retained and strengthened by the highly, but not fully, fluorinated aromatic rings.