Dubackic Marija, Lattanzi Veronica, Liu Yun, Haertlein Michael, Devos Juliette M, Sparr Emma, Linse Sara, Olsson Ulf
Physical Chemistry, Chemistry Centre, Lund University, SE-22100 Lund, Sweden.
Biochemistry and Structural Biology, Chemistry Centre, Lund University, SE-22100 Lund, Sweden.
Soft Matter. 2025 Jan 29;21(5):914-926. doi: 10.1039/d4sm01036a.
We have investigated the adsorption of the amyloid-forming protein α-Synuclein (αSyn) onto small unilamellar vesicles composed of a mixture of zwitterionic POPC and anionic POPS lipids. αSyn monomers adsorb onto the anionic lipid vesicles where they adopt an α-helical secondary structure. The degree of adsorption depends on the fraction of anionic lipid in the mixed lipid membrane, but one needs to consider the electrostatic shift of the serine p with increasing fraction of POPS. The vesicles with adsorbed αSyn monomers are kinetically stable. However, after fibrils have been formed, here triggered by the addition of a small concentration of pre-formed fibrils (seeds), we observed that the average vesicle size increased by approximately a factor of two. This increase in the vesicle size can be explained by vesicle fusion taking place during the fibril formation process.
我们研究了形成淀粉样蛋白的α-突触核蛋白（αSyn）在由两性离子磷脂酰胆碱（POPC）和阴离子磷脂酰丝氨酸（POPS）脂质混合物组成的小单层囊泡上的吸附情况。αSyn单体吸附到阴离子脂质囊泡上，并在那里形成α-螺旋二级结构。吸附程度取决于混合脂质膜中阴离子脂质的比例，但需要考虑随着POPS比例增加丝氨酸p的静电位移。吸附有αSyn单体的囊泡在动力学上是稳定的。然而，在形成纤维后，这里是由添加低浓度的预形成纤维（种子）引发的，我们观察到平均囊泡大小增加了约两倍。囊泡大小的这种增加可以通过纤维形成过程中发生的囊泡融合来解释。
