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纳米孔内单个酶的动力学

Dynamics of single enzymes confined inside a nanopore.

作者信息

Galenkamp Nicole Stéphanie, van den Noort Marco, Maglia Giovanni

机构信息

Chemical Biology, Groningen Biomolecular Sciences & Biotechnology Institute, University of Groningen 9747 AG Groningen The Netherlands

Division of Physical Chemistry, Department of Chemistry, Lund University P.O. Box 124 22100 Lund Sweden.

出版信息

RSC Chem Biol. 2025 Sep 18. doi: 10.1039/d5cb00149h.

DOI:10.1039/d5cb00149h
PMID:40978460
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12445297/
Abstract

Enzymes are powerful catalysts that perform chemical reactions with remarkable speed and specificity. Their intrinsic dynamics often play a crucial role in determining their catalytic properties. To achieve a comprehensive understanding of enzymes, a diverse and sophisticated experimental toolbox capable of studying enzyme dynamics at the single-molecule level is necessary. In this review, we discuss nanopore technology as an emerging and powerful platform in single-molecule enzymology. We demonstrate how nanopores can be employed to probe enzyme dynamics in real-time, and we highlight how these studies have contributed to fundamentally and quantitatively elucidating enzymological concepts, such as allostery and hysteresis. Finally, we explore the potentials and limitations of nanopores in advancing single-molecule enzymology. By presenting the unique possibilities offered by nanopores, we aim to inspire the integration of this technology into future enzymology research.

摘要

酶是强大的催化剂,能以惊人的速度和特异性进行化学反应。它们的内在动力学在决定其催化特性方面往往起着关键作用。为了全面了解酶,需要一个多样化且复杂的实验工具箱,能够在单分子水平上研究酶的动力学。在这篇综述中,我们讨论了纳米孔技术作为单分子酶学中一个新兴且强大的平台。我们展示了纳米孔如何用于实时探测酶的动力学,并强调了这些研究如何在从根本上和定量地阐明诸如变构和滞后等酶学概念方面做出了贡献。最后,我们探讨了纳米孔在推进单分子酶学方面的潜力和局限性。通过展示纳米孔提供的独特可能性,我们旨在激发将这项技术整合到未来的酶学研究中。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed7d/12445297/12a541ea603b/d5cb00149h-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed7d/12445297/a60ee4140146/d5cb00149h-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed7d/12445297/50b606786e32/d5cb00149h-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed7d/12445297/12a541ea603b/d5cb00149h-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed7d/12445297/a60ee4140146/d5cb00149h-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed7d/12445297/50b606786e32/d5cb00149h-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed7d/12445297/12a541ea603b/d5cb00149h-f3.jpg

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本文引用的文献

1
Toward single-molecule protein sequencing using nanopores.迈向使用纳米孔的单分子蛋白质测序
Nat Biotechnol. 2025 Mar;43(3):312-322. doi: 10.1038/s41587-025-02587-y. Epub 2025 Mar 17.
2
Tracking flaviviral protease conformational dynamics by tuning single-molecule nanopore tweezers.通过调节单分子纳米孔镊子追踪黄病毒蛋白酶的构象动力学
Biophys J. 2025 Jan 7;124(1):145-157. doi: 10.1016/j.bpj.2024.11.017. Epub 2024 Nov 22.
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Allostery can convert binding free energies into concerted domain motions in enzymes.变构作用可以将结合自由能转化为酶中的协同结构域运动。
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Multi-pass, single-molecule nanopore reading of long protein strands.多步、单分子纳米孔对长蛋白链的读取。
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Label-Free Mapping of Multivalent Binding Pathways with Ligand-Receptor-Anchored Nanopores.利用配体-受体锚定纳米孔对多价结合途径进行无标记映射
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Magnesium induced structural reorganization in the active site of adenylate kinase.镁诱导的腺苷酸激酶活性位点结构重排。
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Understanding Electrophoresis and Electroosmosis in Nanopore Sensing with the Help of the Nanopore Electro-Osmotic Trap.借助纳米孔电渗阱理解纳米孔传感中的电泳和电渗现象。
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Monomeric Esterase: Insights into Cooperative Behavior, Hysteresis/Allokairy.单体酯酶:合作行为、滞后/变构的洞察。
Biochemistry. 2024 May 7;63(9):1178-1193. doi: 10.1021/acs.biochem.3c00668. Epub 2024 Apr 26.