Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, 78350 Jouy en Josas, France.
Biosens Bioelectron. 2010 Dec 15;26(4):1399-406. doi: 10.1016/j.bios.2010.07.064. Epub 2010 Jul 23.
The molecular mechanism involved in early stages of prion protein (PrP) conversion has been investigated using the chip based SPR technology, focusing on PrP interactions with membranes, either in its monomeric, oligomeric or Cu(II)-ions bound forms. We observed a strong interaction between PrP and cell membrane models of different lipid compositions. Circular dichroism tests show that membrane-bound, oligomerized or Cu(II)-complexed PrP may adopt a β-sheet-rich conformation. Moreover, upon PrP binding membrane vesicles may aggregate and/or be fragmented depending on vesicle net-charge and their lipid/raft composition. The whole study emphasizes the outstanding performance of the on-a-chip approach for the investigation of prion conversion and could be useful for developing sensor formats for prion assessments in biological samples.
使用基于芯片的 SPR 技术研究了朊病毒蛋白 (PrP) 转化早期涉及的分子机制，重点研究了 PrP 与膜的相互作用，无论是在其单体、寡聚体还是 Cu(II)-离子结合形式下。我们观察到 PrP 与不同脂质组成的细胞膜模型之间存在强烈的相互作用。圆二色性测试表明，膜结合的、寡聚化的或 Cu(II)络合的 PrP 可能采用富含β-折叠的构象。此外，根据囊泡的净电荷及其脂质/筏组成，PrP 结合膜囊泡可能会聚集和/或碎片化。整个研究强调了芯片上方法在朊病毒转化研究中的卓越表现，并且对于开发用于生物样品中朊病毒评估的传感器格式可能是有用的。
