Orientation determination of interfacial beta-sheet structures in situ.
Orientation determination of interfacial beta-sheet structures in situ.
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DOI：
10.1021/jp102343h
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发表时间：
2010-07-01
影响因子：
3.3
通讯作者：
Chen, Zhan
中科院分区：
文献类型：
--
作者：
Nguyen, Khoi Tan;King, John Thomas;Chen, Zhan
界面蛋白和肽的取向等结构信息对于理解这些生物分子的性质和功能非常重要，这些生物分子在生物应用和过程中起着至关重要的作用，如抗微生物选择性，膜蛋白活性，生物相容性和生物传感性能。α-螺旋和β-折叠结构是肽和蛋白质中最常见的二级结构。本文首次提出了一种结合衰减全反射傅里叶变换红外光谱（ATR-FTIR）和和频振动光谱（SFG）研究界面β-折叠结构取向的方法。作为该方法的说明，使用常规和手性SFG光谱以及极化ATR-FTIR酰胺I信号来确定鲎素I（具有反平行β折叠的17-氨基酸肽）吸附到聚合物表面以及与脂质双层缔合的取向。确定了界面处β片层的倾角（θ）和扭转角（θ）。该方法可用于复杂分子中β折叠组分的原位结构信息的获取。这种方法与目前用于研究α-螺旋结构的现有方法相结合，将大大拓宽光谱学在物理化学、生物化学、生物物理学和结构生物学中的应用。
Structural information such as orientations of interfacial proteins and peptides is important for understanding properties and functions of such biological molecules, which play crucial roles in biological applications and processes such as antimicrobial selectivity, membrane protein activity, biocompatibility, and biosensing performance. The α-helical and β-sheet structures are the most widely encountered secondary structures in peptides and proteins. In this paper, for the first time, a method to quantify the orientation of the interfacial β-sheet structure using a combined Attenuated Total Reflectance Fourier Transformation Infrared Spectroscopic (ATR-FTIR) and Sum Frequency Generation (SFG) vibrational spectroscopic study was developed. As an illustration of the methodology, the orientation of tachyplesin I, a 17-amino acid peptide with an anti-parallel β-sheet, adsorbed to polymer surfaces as well as associated with a lipid bilayer was determined using the regular and chiral SFG spectra, together with polarized ATR-FTIR amide I signals. Both the tilt angle (θ) and the twist angle (ψ) of the β-sheet at interfaces are determined. The developed method in this paper can be used to obtain in situ structural information of β-sheet components in complex molecules. The combination of this method and the existing methodology that is currently used to investigate α-helical structures will greatly broaden the application of optical spectroscopy in physical chemistry, biochemistry, biophysics, and structural biology.
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影响因子：
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作者：
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通讯作者：
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影响因子：
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作者：
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