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首页> 外文期刊>Biochemistry >A Study of the Regional Effects of alpha-Synuclein on the Organization and Stability of Phospholipid Bilayers
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A Study of the Regional Effects of alpha-Synuclein on the Organization and Stability of Phospholipid Bilayers

机译：α-突触核蛋白对磷脂双层的组织和稳定性的区域影响研究

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Associations between the protein alpha-synuclein (alpha-syn) and presynaptic vesicles have been implicated in synaptic plasticity and neurotransmitter release and may also affect how the protein aggregates into fibrils found in Lewy bodies,the cellular inclusions associated with neurodegenerative diseases.This work investigated how alpha-syn interacts with model phospholipid membranes and examined what effect protein binding has upon the physical properties of lipid bilayers.Wide line ~2H and ~(31)P NMR spectra of phospholipid vesicles revealed that alpha-syn associates with membranes containing lipids with anionic headgroups and can disrupt the integrity of the lipid bilayer,but the protein has little effect on membranes of zwitterionic phosphatidylcholine.A peptide,alpha-syn(10-48),which corresponds to the lysine-rich N-terminal region of alpha-syn,was found to associate with lipid headgroups with a preference for a negative membrane surface charge.Another peptide,alpha-syn(120-140),which corresponds to the glutamate-rich C-terminal region,also associates weakly with lipid headgroups but with a slightly higher affinity for membranes with no net surface charge than for negatively charged membrane surfaces.Binding of alpha-syn-(10-48) and alpha-syn(120-140) to the lipid vesicles did not disrupt the lamellar structure of the membranes,but both peptides appeared to induce the lateral segregation of the lipids into clusters of acidic lipid-enriched and acidic lipid-deficient domains.From these findings,it is speculated that the N-terminal and C-terminal domains of full-length a-syn might act in concert to organize the membrane components during normal protein function and perhaps play a role in presynaptic vesicle synthesis,maintenance,and fusion.
机译：蛋白质α-突触核蛋白（α-syn）和突触前囊泡之间的关联已牵涉到突触可塑性和神经递质释放，还可能影响蛋白质如何聚集成路易体中的原纤维，与神经退行性疾病相关的细胞内含物。 α-syn如何与模型磷脂膜相互作用，并检查蛋白质结合对脂质双层的物理特性有何影响。磷脂小泡的〜2H和〜（31）P NMR宽谱线表明，α-syn与含有脂质的膜结合阴离子头基，可破坏脂质双层的完整性，但该蛋白对两性离子磷脂酰胆碱的膜影响很小。一种肽，α-syn（10-48），对应于富含α-赖氨酸的N-端区域syn，被发现与脂类头基相关，偏向于膜表面带负电荷。另一个肽，α-syn（120-140），对应于富含谷氨酸的C末端区域，也与脂质头基团弱关联，但对无净表面电荷的膜的亲和力比对带负电荷的膜表面的亲和力略高.α-syn-（10-48）和脂质囊泡的α-syn（120-140）不会破坏膜的层状结构，但两种肽似乎都可以诱导脂质的横向偏析成酸性脂质富集和酸性脂质缺陷域的簇。结果发现，全长a-syn的N端和C端结构域可能在蛋白质正常功能期间协同作用，以组织膜成分，并可能在突触前囊泡的合成，维持和融合中发挥作用。

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