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在快速突变的单个病毒刺突蛋白中感知动态演变的短程纳米机械力。

Sensing Dynamically Evolved Short-Range Nanomechanical Forces in Fast-Mutating Single Viral Spike Proteins.

作者信息

Payam Amir Farokh, Funari Riccardo, Scamarcio Gaetano, Bhalla Nikhil

机构信息

Nanotechnology and Integrated Bioengineering Centre (NIBEC) School of Engineering Ulster University York Street Belfast, Northern Ireland, BT15 1AP UK.

Healthcare Technology Hub School of Engineering Ulster University York Street Belfast, Northern Ireland, BT15 1AP UK.

出版信息

Small Sci. 2023 Jun 11;3(8):2300029. doi: 10.1002/smsc.202300029. eCollection 2023 Aug.

DOI:10.1002/smsc.202300029
PMID:40213609
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11935963/
Abstract

Understanding changes in the mechanical features of a single protein from a mutated virus while establishing its relation to the point mutations is critical in developing new inhibitory routes to tackle the uncontrollable spread of the virus. Addressing this, herein, the chemomechanical features of a single spike protein are quantified from alpha, beta, and gamma variants of SARS-CoV-2. Integrated amplitude-modulation atomic force microscopy is used with dynamic force-distance curve (FDC) spectroscopy, in combination with theoretical models, to quantify Young's modulus, stiffness, adhesion forces, van der Waals forces, and the dissipative energy of single spike proteins. These obtained nanomechanical properties can be correlated with mutations in the individual proteins. Therefore, this work opens new possibilities to understand how the mechanical properties of a single spike protein relate to the viral functions. Additionally, single-protein nanomechanical experiments enable a variety of applications that, collectively, may build up a new portfolio of understanding protein biochemistry during the evolution of viruses.

摘要

在确定单个蛋白质的机械特性变化与点突变之间的关系时,了解来自突变病毒的单个蛋白质的机械特性变化对于开发新的抑制途径以应对病毒的失控传播至关重要。针对这一问题,本文通过SARS-CoV-2的α、β和γ变体对单个刺突蛋白的化学机械特性进行了量化。集成振幅调制原子力显微镜与动态力-距离曲线(FDC)光谱联用,并结合理论模型,以量化单个刺突蛋白的杨氏模量、刚度、粘附力、范德华力和耗散能量。这些获得的纳米力学特性可以与单个蛋白质中的突变相关联。因此,这项工作为理解单个刺突蛋白的机械特性如何与病毒功能相关联开辟了新的可能性。此外,单蛋白纳米力学实验能够实现多种应用,这些应用共同可能构建一个在病毒进化过程中理解蛋白质生物化学的新组合。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e37c/11935963/af3cb12df5f5/SMSC-3-2300029-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e37c/11935963/3f6d874735b6/SMSC-3-2300029-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e37c/11935963/f498d3e15662/SMSC-3-2300029-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e37c/11935963/af3cb12df5f5/SMSC-3-2300029-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e37c/11935963/3f6d874735b6/SMSC-3-2300029-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e37c/11935963/f498d3e15662/SMSC-3-2300029-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e37c/11935963/af3cb12df5f5/SMSC-3-2300029-g003.jpg

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