Dynamics of Unfolded Protein Transport through an Aerolysin Pore

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• 作者：Manuela Pastoriza-Gallego ; Leila Rabah ; Gabriel Gibrat ; B茅n茅dicte Thiebot ; Fran莽oise Gisou van der Goot ; Lo茂c Auvray ; Jean-Michel Betton ; Juan Pelta
• 刊名：Journal of the American Chemical Society
• 出版年：2011
• 出版时间：March 9, 2011
• 年：2011
• 卷：133
• 期：9
• 页码：2923-2931
• 全文大小：1136K
• 年卷期：v.133,no.9(March 9, 2011)
• ISSN：1520-5126

文摘

Protein export is an essential mechanism in living cells and exported proteins are usually translocated through a protein-conducting channel in an unfolded state. Here we analyze, by electrical detection, the entry and transport of unfolded proteins, at the single molecule level, with different stabilities through an aerolysin pore, as a function of the applied voltage and protein concentration. The frequency of ionic current blockades varies exponentially as a function of the applied voltage and linearly as a function of protein concentration. The transport time of unfolded proteins decreases exponentially when the applied voltage increases. We prove that the ionic current blockade duration of a double-sized protein is longer than that assessed for a single protein supporting the transport phenomenon. Our results fit with the theory of confined polyelectrolyte and with some experimental results about DNA or synthetic polyelectrolyte translocation through protein channels as a function of applied voltage. We discuss the potential of the aerolysin nanopore as a tool for protein folding studies as it has already been done for 伪-hemolysin.