利用和频振动光谱研究肽在固/液界面的α-螺旋和β-折叠结构。
Probing alpha-helical and beta-sheet structures of peptides at solid/liquid interfaces with SFG.
作者信息
Chen Xiaoyun, Wang Jie, Sniadecki Jason J, Even Mark A, Chen Zhan
机构信息
Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.
出版信息
Langmuir. 2005 Mar 29;21(7):2662-4. doi: 10.1021/la050048w.
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 B1/B3 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 MSI594 alpha-helical structure was observed at the PS/MSI594 solution interface. This research validates SFG as a powerful technique for revealing detailed secondary structures of interfacial proteins and peptides.
我们证明了和频振动光谱（SFG）能够区分吸附在固/液界面的蛋白质或肽的不同二级结构。在聚苯乙烯（PS）/溶液界面处，鲎素I的SFG光谱有一个对应于反平行β折叠的B1/B3模式的指纹峰。加入二硫苏糖醇后，这个峰消失了，因为二硫苏糖醇会破坏β折叠结构。在PS/MSI594溶液界面观察到了指示MSI594α螺旋结构的SFG光谱。这项研究证实了SFG是一种揭示界面蛋白质和肽详细二级结构的强大技术。
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