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首页> 外文期刊>Journal of the American Chemical Society >Nitrogen-14 Solid-State NMR Spectroscopy of Aligned Phospholipid Bilayers to Probe Peptide-Lipid Interaction and Oligomerization of Membrane Associated Peptides
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Nitrogen-14 Solid-State NMR Spectroscopy of Aligned Phospholipid Bilayers to Probe Peptide-Lipid Interaction and Oligomerization of Membrane Associated Peptides

机译：对齐的磷脂双层的氮14固态NMR光谱，以探测肽-脂相互作用和膜相关肽的低聚。

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Characterization of the oligomerization of membrane-associated peptides is important to understand the folding and function of biomolecules like antimicrobial peptides, fusion peptides, amyloid peptides, toxins, and ion channels. However, this has been considered to be very difficult, because the amphipathic properties of the constituents of the cell membrane pose tremendous challenges to most commonly used biophysical techniques. In this study, we present the application of a simple ~(14)N solid-state NMR spectroscopy of aligned model membranes containing a phosphatidyl choline lipid to investigate the oligomerization of membrane-associated peptides. Since the near-symmetric nature of the choline headgroup of a phosphocholine lipid considerably reduces the ~(14)N quadrupole coupling, there are significant practical advantages in using ~(14)N solid-state NMR experiments to probe the interaction of peptide or protein with the surface of model membranes. Experimental results for several membrane-associated peptides are presented in this paper. Our results suggest that the experimentally measured ~(14)N quadrupole splitting of the lipid depends on the peptide-induced changes in the electrostatic potential of the lipid bilayer surface and therefore on the nature of the peptide, peptide-membrane interaction, and peptide-peptide interaction. It is inferred that the membrane orientation and oligomerization of the membrane-associated peptides can be measured using ~(14)N solid-state NMR spectroscopy.
机译：膜相关肽的寡聚化表征对于理解生物分子（如抗菌肽，融合肽，淀粉样肽，毒素和离子通道）的折叠和功能很重要。然而，这被认为是非常困难的，因为细胞膜成分的两亲性质对最常用的生物物理技术提出了巨大的挑战。在这项研究中，我们提出了一个简单的〜（14）N固态NMR光谱学，用于对包含磷脂酰胆碱脂质的对准模型膜进行研究，以研究膜相关肽的寡聚化。由于磷酸胆碱脂质的胆碱首基的近对称性质大大降低了〜（14）N四极偶合，因此使用〜（14）N固态NMR实验来探测肽或蛋白质的相互作用具有明显的实际优势。与模型膜的表面。本文介绍了几种膜相关肽的实验结果。我们的结果表明，实验测得的脂质的〜（14）N四极分裂取决于肽诱导的脂质双层表面静电势的变化，因此取决于肽的性质，肽-膜相互作用和肽-肽相互作用。推断可以使用〜（14）N固态NMR光谱测量膜相关肽的膜取向和寡聚。

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