In situ monitoring of protein transfer into nanoscale channels
In situ monitoring of protein transfer into nanoscale channels
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DOI：
10.1016/j.xcrp.2021.100576
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发表时间：
2021-09
影响因子：
8.9
通讯作者：
Yanxiong Pan;Xiaoliang Wang;Hui Li;Junyu Ren;Yin Zhang;Drew Jordahl;I. Schuster;J. Farmakes;H. Hong;Zhongyu Yang;Shengqian Ma
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作者：
Yanxiong Pan;Xiaoliang Wang;Hui Li;Junyu Ren;Yin Zhang;Drew Jordahl;I. Schuster;J. Farmakes;H. Hong;Zhongyu Yang;Shengqian Ma
蛋白质转移到纳米级的隔室对许多细胞/生命过程至关重要，但关于隔室性质如何影响蛋白质在转移过程中的取向的报道很少。这样的知识差距限制了对蛋白质转移机制的深入了解，这可以用纳米多孔材料来弥补。在这里，我们分别使用介孔二氧化硅、共价有机框架和具有带电、疏水和中性表面的金属-有机框架来阐明通道特性对模型蛋白溶菌酶转移的影响。利用定点自旋标记和时间分辨电子顺磁共振波谱，我们揭示了根据通道性质的不同，溶菌酶的转移可以是一个多步骤的过程，并描述了溶菌酶在转移到每个通道时的相对取向变化。据我们所知，这是对蛋白质转移到不同区室后取向的第一次结构洞察，对合理设计合成材料以宿主酶或模拟细胞区室具有重要意义。
Protein transfer into nanoscale compartments is critical for many cellular/life processes, yet there are few reports on how compartment properties impact the protein orientation during a transfer. Such a knowledge gap limits a deeper understanding of the protein transfer mechanism, which could be bridged using nanoporous materials. Here, we use a mesoporous silica, a covalent organic framework, and a metal-organic framework with charged, hydrophobic, and neutral surfaces, respectively, to elucidate the impact of channel properties on the transfer of a model protein, lysozyme. Using site-directed spin labeling and time-resolved electron paramagnetic resonance spectroscopy, we reveal that the transfer can be a multi-step process depending on channel properties and depict the relative orientation changes of lysozyme upon transfer into each channel. To the best of our knowledge, this is the first structural insight into protein orientation upon transfer into different compartments, meaningful for the rational design of synthetic materials to host enzymes or mimic the cellular compartments.