纳米盘对于膜蛋白的冷冻电镜研究仍然不可或缺。
Nanodiscs remain indispensable for Cryo-EM studies of membrane proteins.
作者信息
Hiotis Giorgos, Notti Ryan Q, Bao Huan, Walz Thomas
机构信息
Laboratory of Molecular Electron Microscopy, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA; Tri-Institutional PhD Program in Chemical Biology, The Rockefeller University, 1300 York Avenue, New York, NY, USA.
Laboratory of Molecular Electron Microscopy, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA; Department of Medicine, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, NY 10065, USA.
出版信息
Curr Opin Struct Biol. 2025 Jun;92:103042. doi: 10.1016/j.sbi.2025.103042. Epub 2025 Apr 8.
Nanodiscs, small discoidal membrane patches stabilized by membrane-scaffold proteins (MSPs), are popular tools to stabilize integral membrane proteins (IMPs) for structural studies by cryogenic electron microscopy (cryo-EM). While nanodiscs provide a near-native membrane environment for the incorporated IMPs, they do not reproduce all characteristics of a native membrane. Also, IMPs must first be purified in detergent before they can be reconstituted into MSP-based nanodiscs, a problem that has been overcome by newer approaches, such as copolymer-based native nanodiscs and cell-derived vesicles. In this review, we argue that despite these advances, MSP-based nanodiscs remain a unique tool for the structural interrogation of IMPs.
纳米盘是由膜支架蛋白（MSP）稳定的小型盘状膜片，是用于通过低温电子显微镜（cryo-EM）进行结构研究来稳定整合膜蛋白（IMP）的常用工具。虽然纳米盘为掺入的IMP提供了近乎天然的膜环境，但它们并不能重现天然膜的所有特征。此外，IMP必须首先在去污剂中纯化，然后才能重构到基于MSP的纳米盘中，这个问题已被诸如基于共聚物的天然纳米盘和细胞衍生囊泡等新方法所克服。在这篇综述中，我们认为尽管有这些进展，但基于MSP的纳米盘仍然是对IMP进行结构研究的独特工具。
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