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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Different Spectral Signatures of Octapeptide 3_(10)- and alpha-Helices Revealed by Two-Dimensional Infrared Spectroscopy
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Different Spectral Signatures of Octapeptide 3_(10)- and alpha-Helices Revealed by Two-Dimensional Infrared Spectroscopy

机译：二维红外光谱显示八肽3_（10）-和α-螺旋的不同光谱特征

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摘要

Femtosecond two-dimensional infrared (2DIR) spectroscopy is applied to the amide I modes of the terminally protected homo-octapeptide Z-[L-(alpha Me)Val]_8-OtBu in CDCl_3,2,2,2-trifluoroethanol (TFE),and 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) solutions to acquire 2D spectral signatures that distinguish between 3_(10)- and alpha-helix structures.Suppression of diagonal peaks by controlling polarizations of IR pulses clearly reveals cross-peak patterns that are crucial for structural determination.A doublet feature is observed when the peptide ester forms a 3_(10)-helix in CDC1_3 and TFE and when it is at the initial stage of 3m- to a-helix transition in HFIP.In contrast,the 2D IR spectrum shows a multiple peak pattern after the peptide ester has acidolyzed and become an alpha-helix in HFIP.Electronic circular dichroism spectra accompanying the acidolysis-driven conformational change are also reported.This is the first report on the experimental 2D IR signature of a 3_(10)-helical peptide.These results,using a model octapeptide,demonstrate the powerful capability of 2D IR spectroscopy to discriminate between different helical structures.
机译：飞秒二维红外（2DIR）光谱应用于CDCl_3,2,2,2-三氟乙醇（TFE）中末端受保护的同八肽Z- [L-（αMe）Val] _8-OtBu的酰胺I模式，1,1,1,3,3,3-六氟-2-丙醇（HFIP）解决方案，以获取区分3_（10）-和α-螺旋结构的2D光谱特征。通过控制偏振来抑制对角峰红外脉冲清楚地揭示了对结构确定至关重要的跨峰模式。当肽酯在CDC1_3和TFE中形成3_（10）-螺旋并且处于3m-至a-的初始阶段时，观察到双峰特征。相比之下，在肽酯酸化并成为HFIP中的α-螺旋后，二维IR光谱显示出多个峰型。还报道了伴随酸解驱动的构象变化的电子圆二色性光谱。关于3_（10）螺旋肽的实验2D IR签名的第一份报告这些结果使用八肽模型证明了2D红外光谱技术能够区分不同的螺旋结构的强大功能。

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