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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Membrane Disruption Mechanism of a Prion Peptide (106-126) Investigated by Atomic Force Microscopy, Raman and Electron Paramagnetic Resonance Spectroscopy
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Membrane Disruption Mechanism of a Prion Peptide (106-126) Investigated by Atomic Force Microscopy, Raman and Electron Paramagnetic Resonance Spectroscopy

机译：用原子力显微镜，拉曼和电子顺磁共振光谱研究的朊病毒肽（106-126）的膜破坏机制

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摘要

A fragment of the human prion protein spanning residues 106-126 (PrP106-126) recapitulates many essential properties of the disease-causing protein such as amyloidogenicity and cytotoxicity. PrP106-126 has an amphipathic characteristic that resembles many antimicrobial peptides (AMPs). Therefore, the toxic effect of PrP106-126 could arise from a direct association of monomeric peptides with the membrane matrix. Several experimental approaches are employed to scrutinize the impacts of monomeric PrP106-126 on model lipid membranes. Porous defects in planar bilayers are observed by using solution atomic force microscopy. Adding cholesterol does not impede defect formation. A force spectroscopy experiment shows that PrP106-126 reduces Young's modulus of planar lipid bilayers. We use Raman microspectroscopy to study the effect of PrP106-126 on lipid atomic vibrational dynamics. For phosphatidylcholine lipids, PrP106-126 disorders the intrachain conformation, while the interchain interaction is not altered; for phosphatidylethanolamine lipids, PrP106-126 increases the interchain interaction, while the intrachain conformational order remains similar. We explain the observed differences by considering different modes of peptide insertion. Finally, electron paramagnetic resonance spectroscopy shows that PrP106-126 progressively decreases the orientational order of lipid acyl chains in magnetically aligned bicelles. Together, our experimental data support the proposition that monomeric PrP106-126 can disrupt lipid membranes by using similar mechanisms found in AMPs.
机译：人朊蛋白跨越残留物106-126（PRP106-126）的片段概括了疾病导致蛋白质如淀粉样蛋白和细胞毒性的许多基本性质。 PRP106-126具有类似于许多抗微生物肽（AMPS）的两亲性特征。因此，PRP106-126的毒性效果可以从单体肽与膜基质的直接结合产生。使用几种实验方法来仔细审查单体PRP106-126对模型脂膜的影响。通过使用溶液原子力显微镜观察平面双层的多孔缺陷。添加胆固醇不会阻碍缺陷地层。力光谱实验表明，PRP106-126降低了平面脂质双层的杨氏模量。我们使用拉曼微穴位检查来研究PRP106-126对脂质原子振动动力学的影响。对于磷脂酰胆碱脂质，PRP106-126疾病封闭构象，而交流相互作用不会改变;对于磷脂酰乙醇胺脂质，PRP106-126增加了间隔相互作用，而夹紧构象顺序保持相似。通过考虑不同的肽插入方式，我们解释了观察到的差异。最后，电子顺磁共振光谱表明，PRP106-126逐渐降低磁对准双裂纹中脂质酰基链的定位顺序。我们的实验数据支持单体PRP106-126通过使用在安培中发现的类似机制来破坏脂质膜的命题。

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