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首页> 外文期刊>Journal of Molecular Biology >Binding of prion protein to lipid membranes and implications for prion conversion.
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Binding of prion protein to lipid membranes and implications for prion conversion.

机译：ion病毒蛋白与脂质膜的结合及其对病毒转化的影响。

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摘要

The binding of the Syrian hamster prion protein, SHaPrP(90-231), to model lipid membranes was investigated by tryptophan fluorescence. Membranes composed of negatively charged or zwitterionic lipids, and raft-like membranes containing dipalmitoylphosphatidylcholine(1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), cholesterol and sphingomyelin, were investigated. It was found that SHaPrP(90-231) binds to negatively charged lipid membranes and raft-like membranes. Binding of PrP to negatively charged lipid membranes involves both electrostatic and hydrophobic lipid-protein interactions and results in partial insertion of PrP into the lipid bilayer. This membrane-inserted conformation of PrP is richer in beta-sheet structure and has a disruptive effect on the integrity of the lipid bilayer, leading to total release of vesicle contents. In contrast, the binding of PrP to raft-like membranes is driven by hydrophobic lipid-protein interactions and induces the formation of alpha-helical structure. This conformation of PrP with a high content of alpha-helix is formed only at pH 7 and does not destabilize the lipid bilayer. Our findings support the view that an interaction of PrP with lipid membranes could play a role in PrP conversion.
机译：通过色氨酸荧光研究了叙利亚仓鼠pr病毒蛋白SHaPrP（90-231）与脂质膜的结合。研究了由带负电荷或两性离子脂质组成的膜以及含有二棕榈酰磷脂酰胆碱（1,2-二棕榈酰-sn-甘油-3-磷酸胆碱（DPPC），胆固醇和鞘磷脂）的筏状膜，发现SHaPrP（90-231） ）与带负电的脂质膜和筏状膜结合，PrP与带负电的脂质膜结合涉及静电和疏水性脂质-蛋白质相互作用，并导致部分PrP插入脂质双层中。 β-折叠结构更丰富，对脂质双层的完整性具有破坏性作用，导致囊泡内容物的完全释放;相反，PrP与筏状膜的结合是由疏水性脂质-蛋白质相互作用驱动的，并诱导具有高含量的α-螺旋的PrP的这种构象仅在pH 7时形成，并且不会使脂质双层不稳定。我们的发现支持这样的观点，即PrP与脂质膜的相互作用可能在PrP转化中起作用。

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