Short polyethylene glycol chains densely bound to soft nanotube channels for inhibition of protein aggregation
Short polyethylene glycol chains densely bound to soft nanotube channels for inhibition of protein aggregation
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DOI：
10.1039/c6ra06793j
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发表时间：
2016-01-01
期刊：
影响因子：
3.9
通讯作者：
Masuda, M.
中科院分区：
文献类型：
--
作者：
Kameta, N.;Matsuzawa, T.;Masuda, M.
两种不同脂质和短聚乙二醇 (PEG) 单元的两步自组装选择性地产生了具有 7-9 nm 直径纳米通道的分子单层纳米管，纳米通道由短 PEG 链密集功能化。使用环境响应探针的荧光光谱和显微镜表明，当温度升高到 45-50 摄氏度以上时，纳米通道中的 PEG 链会脱水，并通过冷却至 25 摄氏度进行再水化，而本体溶液中的 PEG 链则没有表现出响应温度变化的这种脱水/再水化行为。由于内部 PEG 链脱水而变得疏水的纳米管通道有效地抑制了高温条件下热变性蛋白质的聚集。通过内部 PEG 链的再水化实现亲水性纳米通道的再生，使封装的蛋白质能够快速释放到本体溶液中，同时促进蛋白质的重折叠。
Two-step self-assembly of two different lipids and a short polyethylene glycol ( PEG) unit selectively produced molecular monolayer nanotubes with 7-9 nm-diameter nanochannels densely functionalized with short PEG chains. Fluorescence spectroscopy and microscopy using an environmentally responsive probe suggested that the PEG chains in the nanochannel were dehydrated when the temperature was raised above 45-50 degrees C and rehydrated by cooling to 25 degrees C, whereas the PEG chains in the bulk solution showed no such dehydration/rehydration behavior in response to variations of temperature. Nanotube channels that became hydrophobic as a result of the dehydration of the interior PEG chains effectively suppressed aggregation of a thermally denatured protein under high temperature conditions. Regeneration of the hydrophilic nanochannels by rehydration of the interior PEG chains allowed the encapsulated protein to be quickly released to the bulk solution and simultaneously facilitated the refolding of the protein.