Electrostatic Interaction between SARS-CoV-2 and Charged Surfaces: Spike Protein Evolution Changed the Game

Previous works show the key role of electrostatics in the SARS-CoV-2 virus in aspects such as virus-cell interactions or virus inactivation by ionic surfactants. Electrostatic interactions depend strongly on the variant since the charge of the Spike protein (responsible for virus-environment interactions) evolved across the variants from the highly negative Wild Type (WT) to the highly positive Omicron variant. The distribution of the charge also evolved from diffuse to highly localized. These facts suggest that SARS-CoV-2 should interact strongly with charged surfaces in a way that changed during the virus evolution. This question is studied here by computing the electrostatic interaction between WT, Delta and Omicron Spike proteins with charged surfaces using a new method (based on Debye-Hückel theory) that provides efficiently general results as a function of the surface charge density σ. We found that the interaction of the WT and Delta variant spikes with charged surfaces is dominated by repulsive image forces proportional to σ<sup>2</sup> originating at the protein/water interface. On the contrary, the Omicron variant shows a distinct behavior, being strongly attracted to negatively charged surfaces and repelled from positively charged ones. Therefore, the SARS-CoV-2 virus has evolved from being repelled by charged surfaces to being efficiently adsorbing to negatively charged ones.

Authors

Institutions

Publication Details

Journal
Journal of Chemical Information and Modeling
Published
2024-12-26
DOI
https://doi.org/10.1021/acs.jcim.4c01724
Citations
6
Primary Topic
Protein Structure and Dynamics
Type
article
Field-Weighted Citation Impact
1.40

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Electrostatic Interaction between SARS-CoV-2 and Charged Surfaces: Spike Protein Evolution Changed the Game

Jordi Faraudo, Marc Domingo, Matej Kanduč, Horacio V. Guzman
6 citations
Journal of Chemical Information and Modeling
Protein Structure and Dynamics
1.40
article

Electrostatic Interaction between SARS-CoV-2 and Charged Surfaces: Spike Protein Evolution Changed the Game

Jordi Faraudo, Marc Domingo, Matej Kanduč, Horacio V. Guzman
article en
6 citations

Abstract

Previous works show the key role of electrostatics in the SARS-CoV-2 virus in aspects such as virus-cell interactions or virus inactivation by ionic surfactants. Electrostatic interactions depend strongly on the variant since the charge of the Spike protein (responsible for virus-environment interactions) evolved across the variants from the highly negative Wild Type (WT) to the highly positive Omicron variant. The distribution of the charge also evolved from diffuse to highly localized. These facts suggest that SARS-CoV-2 should interact strongly with charged surfaces in a way that changed during the virus evolution. This question is studied here by computing the electrostatic interaction between WT, Delta and Omicron Spike proteins with charged surfaces using a new method (based on Debye-Hückel theory) that provides efficiently general results as a function of the surface charge density σ. We found that the interaction of the WT and Delta variant spikes with charged surfaces is dominated by repulsive image forces proportional to σ<sup>2</sup> originating at the protein/water interface. On the contrary, the Omicron variant shows a distinct behavior, being strongly attracted to negatively charged surfaces and repelled from positively charged ones. Therefore, the SARS-CoV-2 virus has evolved from being repelled by charged surfaces to being efficiently adsorbing to negatively charged ones.

Journal of Chemical Information and ModelingVol. 65(1)
Jožef Stefan Institute (SI), Institut de Ciència de Materials de Barcelona (ES), Universidad Autónoma de Madrid (ES)
Ministerio de Ciencia, Innovación y Universidades, Javna Agencija za Raziskovalno Dejavnost RS, Ministerio de Ciencia e Innovación, Agència de Gestió d'Ajuts Universitaris i de Recerca, Agencia Estatal de Investigación
Openalex Percentile: Top 18%
Protein Structure and Dynamics
1.40
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.