Most of the ongoing projects aimed at the development of specific therapies and vaccines against COVID-19 use the SARS-CoV-2 spike (S) protein as the main target [1-3]. The binding of the spike protein with the ACE2 receptor (ACE2) of the host cell constitutes the first and key step for virus entry. During this process, the receptor binding domain (RBD) of the S protein plays an essential role, since it contains the receptor binding motif (RBM), responsible for the docking to the receptor. So far, mostly biochemical methods are being tested in order to prevent binding of the virus to ACE2 [4]. Here we show, with the help of atomistic simulations, that external electric fields of easily achievable and moderate strengths can dramatically destabilise the S protein, inducing long-lasting structural damage. One striking field-induced conformational change occurs at the level of the recognition loop L3 of the RBD where two parallel beta sheets, believed to be responsible for a high affinity to ACE2 [5], undergo a change into an unstructured coil, which exhibits almost no binding possibilities to the ACE2 receptor (Figure 1a). Remarkably, while the structural flexibility of S allows the virus to improve its probability of entering the cell, it is also the origin of the surprising vulnerability of S upon application of electric fields of strengths at least two orders of magnitude smaller than those required for damaging most proteins. Our findings suggest the existence of a clean physical method to weaken the SARS-CoV-2 virus without further biochemical processing. Moreover, the effect could be used for infection prevention purposes and also to develop technologies for in-vitro structural manipulation of S. Since the method is largely unspecific, it can be suitable for application to mutations in S, to other proteins of SARS-CoV-2 and in general to membrane proteins of other virus types.
One-step, Wash-free, Nanoparticle Clustering-based Magnetic Particle Spectroscopy (MPS) Bioassay Method for Detection of SARS-CoV-2 Spike and Nucleocapsid Proteins in Liquid Phase
Evaluation of Peppermint Leaf Flavonoids as SARS-CoV-2 Spike Receptor-Binding Domain Attachment Inhibitors to the Human ACE2 Receptor: A Molecular Docking Study
Institute of Physics, University of Brasília（巴西利亚大学物理研究所）；Department of Electrical Engineering, University of Brasília（巴西利亚大学电气工程系）
An effective approach to reduce the penetration potential of Sars-Cov-2 and other viruses by spike protein: Through surface particle electrostatic charge negotiation
本文的目的是提供一个数学模型，以构建一个屏障，可能是有用的，以防止不同的病毒（例如）的渗透。SARS-COV-2）以及带电气溶胶通过静电电荷协商的概念。（相反类型电荷的融合和相似类型电荷的排斥）。在回顾了不同作者在不同实验条件下对不同气溶胶的电荷、表面电荷密度（σ）、电荷迁移率（μ）和静电势的研究的基础上，我们还对不同RNA和DNA病毒（包括SARS-COV-2）的S蛋白的供电子和受电子（供空穴）性质进行了类似的深入研究。根据不同尺寸粒子的电子输运特性，建立了不同尺寸粒子在不同静电场下的穿透电势数学模型。已经进行了深入的研究，以找出由于电子的表面发射（SEE）而产生的静电荷，当导电材料如丝绸，尼龙或羊毛与Gr IV元素如锗或硅摩擦时，它在外部导电表面和内部半导体表面中产生相反的电荷层，由介电材料隔开。这种相反的电荷势垒可以被认为是反型层（IL）。在Gr IV Ge之间的层中积累的静电荷足以融合或排斥RNA、DNA病毒（包括SARS-Cov-2（RNA病毒））或气溶胶的刺突蛋白的电荷。
Quantitative Prediction of Protein-Polyelectrolyte Binding Thermodynamics: Adsorption of Heparin-Analog Polysulfates to the SARS-CoV-2 Spike Protein RBD
Comparative performance of three optical biosensing platforms for SARS-CoV-2 antibodies detection in human serum
SAPIENZA Università di Roma（罗马大学）；Italian Institute of Technology, Centre for Life Nano and Neuro Science（意大利理工学院生命纳米与神经科学中心）；Fraunhofer Institute for Applied Optics and Precision Engineering IOF（弗劳恩霍夫应用光学和精密工程研究所）；University of Rochester（罗切斯特大学）
From atomic to global connectivity in the structure of the SARS-CoV2-Human ACE2 receptor complex
Los Alamos National Laboratory（洛斯阿拉莫斯国家实验室）；Indian Institute of Science（印度科学学院）；University of Regina（里贾纳大学）；Yale University（耶鲁大学）；University of Illinois at Urbana-Champaign（伊利诺伊大学厄巴纳-香槟分校）
Breath analysis by ultra-sensitive broadband laser spectroscopy detects SARS-CoV-2 infection
JILA（JILA研究所）；National Institute of Standards and Technology（美国国家标准与技术研究院）；University of Colorado（科罗拉多大学）；University of Basel（巴塞尔大学）；BioFrontiers Institute（生物前沿研究所）；University of Colorado Anschutz Medical Campus（科罗拉多大学安舒茨医学校区）
