Probing α-helical and β-sheet structures of peptides at solid/liquid interfaces with SFG

被引：117

作者：

Chen, XY ^{[1
]}

Wang, J ^{[1
]}

Sniadecki, JJ ^{[1
]}

Even, MA ^{[1
]}

Chen, Z ^{[1
]}

机构：

[1] Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA

来源：

LANGMUIR | 2005年 / 21卷 / 07期

关键词：

D O I：

10.1021/la050048w

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We demonstrated that sum frequency generation (SFG) vibrational spectroscopy can distinguish different secondary structures of proteins or peptides adsorbed at solid/liquid interfaces. The SFG spectrum for tachyplesin I at the polystyrene (PS)/solution interface has a fingerprint peak corresponding to the B-1/B-3 mode of the antiparallel beta-sheet. This peak disappeared upon the addition of dithiothreitol, which can disrupt the beta-sheet structure. The SFG spectrum indicative of the MS1594 alpha-helical structure was observed at the PS/MS1594 solution interface. This research validates SFG as a powerful technique for revealing detailed secondary structures of interfacial proteins and peptides.

引用

页码：2662 / 2664

页数：3

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