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首页> 美国卫生研究院文献>Biophysical Journal >In situ study by polarization modulated Fourier transform infrared spectroscopy of the structure and orientation of lipids and amphipathic peptides at the air-water interface.
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In situ study by polarization modulated Fourier transform infrared spectroscopy of the structure and orientation of lipids and amphipathic peptides at the air-water interface.

机译：通过极化调制傅里叶变换红外光谱原位研究空气-水界面处脂质和两亲性肽的结构和取向。

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摘要

Free amphipathic peptides and peptides bound to dimyristoylphosphatidylcholine (DMPC) were studied directly at the air/water interface using polarization modulation infrared reflection absorption spectroscopy (PMIRRAS). Such differential reflectivity measurements proved to be a sensitive and efficient technique to investigate in situ the respective conformations and orientations of lipid and peptide molecules in pure and mixed films. Data obtained for melittin, a natural hemolytic peptide, are compared to those of L15K7, an ideally amphipathic synthetic peptide constituted by only apolar Leu and polar Lys residues. For pure peptidic films, the intensity, shape, and position of the amide I and II bands indicate that the L15K7 peptide adopts a totally alpha-helical structure, whereas the structure of melittin is mainly alpha-helical and presents some unordered domains. The L15K7 alpha-helix axis is oriented essentially parallel to the air-water interface plane; it differs for melittin. When injected into the subphase, L15K7 and melittin insert into preformed expanded DMPC monolayers and can be detected by PMIRRAS, even at low peptide content (> 50 DMPC molecules per peptide). In such conditions, peptides have the same secondary structure and orientation as in pure peptidic films.
机译：使用偏振调制红外反射吸收光谱法（PMIRRAS）直接在空气/水界面处研究了游离的两亲性肽和与二肉豆蔻酰磷脂酰胆碱（DMPC）结合的肽。事实证明，这种差分反射率测量是一种灵敏而有效的技术，可用于原位研究纯膜和混合膜中脂质和肽分子的各自构象和取向。将蜂毒肽（一种天然的溶血肽）获得的数据与L15K7（一种仅由非极性Leu和极性Lys残基组成的理想两亲性合成肽）的数据进行比较。对于纯肽膜，酰胺I和II谱带的强度，形状和位置表明L15K7肽采用完全为α螺旋的结构，而蜂毒肽的结构主要为α螺旋并且存在一些无序结构域。 L15K7α-螺旋轴的方向基本上平行于空气-水界面平面；它与蜂毒素不同。当注入亚相时，L15K7和蜂毒肽插入预先形成的扩展DMPC单层，即使在低肽含量（每个肽> 50个DMPC分子）下也可以通过PMIRRAS检测。在这种条件下，肽具有与纯肽膜相同的二级结构和取向。

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