Cytotoxicity of prion protein-derived cell-penetrating peptides is modulated by pH but independent of amyloid formation

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• 作者：Vineeth Mukundan^a ; Christy Maksoudian^a ; Maria C. Vogel^a ; Ibrahim Chehade^a ; Marios S. Katsiotis^b ; Saeed M. Alhassan^b ; Mazin Magzoub^a ; ^{mazin.magzoub@nyu.edu}
• 关键词：Aggregation ; Amyloid ; Cell-penetrating peptides ; Cytotoxicity ; Membrane perturbation ; Prion protein
• 刊名：Archives of Biochemistry and Biophysics
• 出版年：2017
• 出版时间：1 January 2017
• 年：2017
• 卷：613
• 期：Complete
• 页码：31-42
• 全文大小：1880 K
• 卷排序：613

文摘

Toxicity of the prion protein-derived peptides is independent of amyloid formation. Toxicity of mPrP1-28 and bPrP1-30 is due to oligomeric or non-fibrillar assemblies. Toxicity of the peptides is attributed to plasma membrane perturbation. Low pH inhibits ordered aggregation of the peptides and abrogates their toxicity. Under non-toxic conditions, the peptides accumulate in late endosomes/lysosomes.