Lundberg P, Magzoub M, Lindberg M, Hällbrink M, Jarvet J, Eriksson L E G, Langel U, Gräslund A
Department of Neurochemistry and Neurotoxicology, Stockholm University, SE-106 91, Stockholm, Sweden.
Biochem Biophys Res Commun. 2002 Nov 22;299(1):85-90. doi: 10.1016/s0006-291x(02)02595-0.
The N-terminal (1-28) part of the mouse prion protein (PrP) is a cell penetrating peptide, capable of transporting large hydrophilic cargoes through a cell membrane. Confocal fluorescence microscopy shows that it transports the protein avidin (67kDa) into several cell lines. The (1-28) peptide has a strong tendency for aggregation and beta-structure formation, particularly in interaction with negatively charged phospholipid membranes. The findings have implications for how prion proteins with uncleaved signal peptides in the N-termini may enter into cells, which is important for infection. The secondary structure conversion into beta-structure may be relevant as a seed for the conversion into the scrapie (PrP(Sc)) form of the protein and its amyloidic transformation.
小鼠朊病毒蛋白（PrP）的N端（1-28）部分是一种细胞穿透肽，能够通过细胞膜转运大型亲水性货物。共聚焦荧光显微镜显示，它能将抗生物素蛋白（67kDa）转运到几种细胞系中。（1-28）肽具有强烈的聚集倾向和β结构形成趋势，特别是在与带负电荷的磷脂膜相互作用时。这些发现对于N端带有未切割信号肽的朊病毒蛋白如何进入细胞具有重要意义，而这对于感染至关重要。二级结构转化为β结构可能作为该蛋白转化为羊瘙痒病（PrP(Sc)）形式及其淀粉样转化的种子。
