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首页> 外文期刊>Biochemistry >Structural properties of the putative fusion peptide of fertilin, a protein active in sperm-egg fusion, upon interaction with the lipid bilayer
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Structural properties of the putative fusion peptide of fertilin, a protein active in sperm-egg fusion, upon interaction with the lipid bilayer

机译:推定的铁蛋白融合肽的结构特性,这种蛋白在与脂双层相互作用时具有精子-卵融合活性。

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摘要

We recently demonstrated that a peptide representing the putative fusion domain of fertilin, a surface membrane protein of sperm involved in sperm-egg fusion, induces fusion of large unilamellar vesicles containing negatively charged lipids [Martin, I., and Ruysschaert, J, M. (1997) FEES Lett. 405, 351-355], In the present work, we demonstrate that increasing the concentration in negatively charged lipids strongly enhances the binding of the fertilin fusion peptide to the membrane, suggesting that electrostatic attractions play a crucial role in the binding process. While no significant change of the secondary structure content is observed by increasing the amounts of negatively charged lipids in the bilayer, the orientation of the alpha-helix changes from a parallel to an oblique orientation in the membrane. This topological change is confirmed by amide II hydrogen/deuterium exchange measurements that monitor the accessibility of the peptide to the water medium. Differential scanning calorimetry data also suggest that the fertilin fusion peptide lowers the bilayer to hexagonal phase transition temperature of model membranes composed of mixtures of dipalmitoleoylphosphatidylethanolamine and 1-palmitoyl-2-oleoylphosphatidylserine and therefore promotes negative curvature in Lipid vesicles. A comparison of the biophysical properties and the membrane-perturbing activities of fertilin and of viral fusion peptides is discussed in terms of sperm-egg fusion and virus cell fusion. [References: 50]
机译:我们最近证明了代表假定的铁蛋白融合结构域的一种肽,该蛋白是参与精子-卵融合的精子表面膜蛋白,可诱导含有带负电荷脂质的单层大囊泡融合[Martin,I.,and Ruysschaert,J,M. (1997)FEES Lett。 405,351-355],在目前的工作中,我们证明了增加带负电荷的脂质的浓度会大大增强铁蛋白融合肽与膜的结合,这表明静电吸引力在结合过程中起着至关重要的作用。虽然通过增加双层中带负电荷的脂质的量没有观察到二级结构含量的显着变化,但α-螺旋的方向从膜中的平行方向变为倾斜方向。通过监测肽对水介质的可及性的酰胺II氢/氘交换测量结果证实了这种拓扑变化。差示扫描量热法数据还表明,铁蛋白融合肽降低了由二棕榈油酰基磷脂酰乙醇胺和1-棕榈酰基-2-油酰基磷脂酰丝氨酸的混合物组成的模型膜的双层至六边形相变温度,因此促进了脂质囊泡的负曲率。从精卵融合和病毒细胞融合的角度讨论了铁蛋白和病毒融合肽的生物物理特性和膜扰动活性的比较。 [参考:50]

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