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首页> 外文学位 >Studies of interactions between peptides/proteins and lipid bilayers using sum frequency generation vibrational spectroscopy.
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Studies of interactions between peptides/proteins and lipid bilayers using sum frequency generation vibrational spectroscopy.

机译：使用总频率生成振动光谱研究肽/蛋白质与脂质双层之间的相互作用。

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摘要

The orientation of peptides and proteins on surfaces can have drastic implications on the function of these interfacial molecules. Interfacial proteins and peptides can play crucial roles in biological applications and processes such as antimicrobial selectivity, membrane protein activity, biocompatibility, and biosensing performance. The alpha-helical and beta-sheet structures are the most widely encountered secondary structures in peptides and proteins. The orientation of interfacial alpha-helical and beta-sheet structure can be determined using a combination of linear and second order nonlinear optical vibrational spectroscopies, namely Attenuated Total Reflectance Fourier Transformation Infrared Spectroscopy (ATR-FTIR) and Sum Frequency Generation (SFG) vibrational spectroscopy. Here in this dissertation, orientation determination methods of the interfacial alpha-helical, 3-10 helical and beta-sheet structures, using the combined ATR-FTIR and SFG spectroscopic techniques, have been systematically developed. SFG was used to probe multiple amide I vibrational modes, which are related to their respective molecular hyperpolarizability tensor components through the orientation of the studied secondary structures. By implementing the bond additivity model along with group theory, the molecular hyperpolarizability tensor was determined for the SFG active vibrational modes of the secondary structures from the calculated IR transition dipole moment and the Raman polarizability tensor. The SFG susceptibility ratio of the signals collected in different polarization combinations, together with polarized ATR-FTIR amide I signals, can be used to determine the orientation angles of the interfacial secondary structures being studied. As an illustration of the methodology, the orientations of magainin 2 (an alpha-helical peptide), Cytochrome b5 (an alpha-helical structure containing protein), tachyplesin I (a beta-sheet peptide), at various interfaces were determined.
机译：肽和蛋白质在表面上的取向可能对这些界面分子的功能产生重大影响。界面蛋白和肽可以在生物学应用和过程中发挥关键作用，例如抗菌选择性，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使用最广泛的二级结构。可以使用线性和二阶非线性光学振动光谱法（即衰减全反射傅立叶变换红外光谱（ATR-FTIR）和和频率生成（SFG）振动光谱法）的组合来确定界面α-螺旋和β-sheet结构的方向。 。在本文中，系统地研究了结合ATR-FTIR和SFG光谱技术确定界面α-螺旋，3-10螺旋和β-折叠结构的取向的方法。 SFG用于探测多种酰胺I的振动模式，这些振动模式通过研究的二级结构的取向与其各自的分子超极化张量分量相关。通过结合基团理论实现键加性模型，从计算的IR跃迁偶极矩和拉曼极化率张量确定了二级结构的SFG主动振动模态的分子超极化率张量。在不同的极化组合中收集到的信号的SFG磁化率，以及极化的ATR-FTIR酰胺I信号，可以用来确定所研究的界面二级结构的取向角。作为方法的说明，确定了在各种界面上的magainin 2（α-螺旋肽），细胞色素b5（包含蛋白质的α-螺旋结构），tachyplesin I（β-sheet肽）的方向。

著录项

  • 作者

    Nguyen, Khoi Tan.;

  • 作者单位

    University of Michigan.;

  • 授予单位 University of Michigan.;
  • 学科 Chemistry Physical.
  • 学位 Ph.D.
  • 年度 2010
  • 页码 157 p.
  • 总页数 157
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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