Sette-de-Souza PH, Fernandes Costa MJ, Dutra Borges BC. SARS-CoV-2 proteins show great binding affinity to resin composite monomers and polymerized chains. World J Exp Med 2025; 15(1): 94022 [DOI: 10.5493/wjem.v15.i1.94022]
Corresponding Author of This Article
Pedro Henrique Sette-de-Souza, DDS, MSc, PhD, Full Professor, Faculdade de Odontologia, Universidade de Pernambuco-campus Arcoverde, Rua Cícero Monteiro de Melo, s/n-São Cristóvão, Arcoverde/PE, Arcoverde 56503-146, Pernambuco, Brazil. pedro.souza@upe.br
Research Domain of This Article
Microbiology
Article-Type of This Article
Basic Study
Open-Access Policy of This Article
This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Pedro Henrique Sette-de-Souza, Moan Jéfter Fernandes Costa, Faculdade de Odontologia, Universidade de Pernambuco-campus Arcoverde, Arcoverde 56503-146, Pernambuco, Brazil
Pedro Henrique Sette-de-Souza, Programa de Pós-Graduação em Saúde e Desenvolvimento Socioambiental, Universidade de Pernambuco-campus Garanhuns, Garanhuns 55294-902, Pernambuco, Brazil
Moan Jéfter Fernandes Costa, Programa de Pós-Graduação em Biologia Celular e Molecular Aplicada, Universidade de Pernambuco-campus Santo Amaro, Recife 50100-130, Pernambuco, Brazil
Boniek Castillo Dutra Borges, Department of Odontologia, Universidade Federal do Rio Grande do Norte, Natal 59056-000, Rio Grande do Norte, Brazil
Boniek Castillo Dutra Borges, Programa de Pós-Graduação em Ciências Odontológicas, Universidade Federal do Rio Grande do Norte, Natal 59056-000, Rio Grande do Norte, Brazil
Author contributions: Sette-de-Souza PH, Fernandes Costa MJ and Dutra Borges BC designed, performed the experiments, acquired, analyzed, and interpreted the data; all of the authors wrote the manuscript and approved the final version of the article.
Supported by The Coordenação de Aperfeiçoamento de Pessoal de Nível Superior-Brasil (CAPES), No. 001.
Conflict-of-interest statement: All authors declare no conflict of interest in publishing the manuscript.
Data sharing statement: Request to the corresponding author.
Open-Access: This article is an open-access article that was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution NonCommercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: https://creativecommons.org/Licenses/by-nc/4.0/
Corresponding author: Pedro Henrique Sette-de-Souza, DDS, MSc, PhD, Full Professor, Faculdade de Odontologia, Universidade de Pernambuco-campus Arcoverde, Rua Cícero Monteiro de Melo, s/n-São Cristóvão, Arcoverde/PE, Arcoverde 56503-146, Pernambuco, Brazil. pedro.souza@upe.br
Received: March 10, 2024 Revised: October 3, 2024 Accepted: October 30, 2024 Published online: March 20, 2025 Processing time: 291 Days and 7.6 Hours
Abstract
BACKGROUND
Due to saliva and salivary glands are reservoir to severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2), aerosols and saliva droplets are primary sources of cross-infection and are responsible for the high human–human transmission of SARS-CoV-2. However, there is no evidence about how SARS-CoV-2 interacts with oral structures, particularly resin composites.
AIM
To evaluate the interaction of SARS-CoV-2 proteins with monomers present in resin composites using in silico analysis.
METHODS
Four SARS-CoV-2 proteins [i.e. main protease, 3C-like protease, papain-like protease (PLpro), and glycoprotein spike] were selected along with salivary amylase as the positive control, and their binding affinity with bisphenol-A glycol dimethacrylate, bisphenol-A ethoxylated dimethacrylate, triethylene glycol dimethacrylate, and urethane dimethacrylate was evaluated. Molecular docking was performed using AutoDock Vina and visualised in Chimera UCSF 1.14. The best ligand–protein model was identified based on the binding energy (ΔG–kcal/moL).
RESULTS
Values for the binding energies ranged from -3.6 kcal/moL to -7.3 kcal/moL. The 3-monomer chain had the lowest binding energy (i.e. highest affinity) to PLpro and the glycoprotein spike. Non-polymerised monomers and polymerised chains interacted with SARS-CoV-2 proteins via hydrogen bonds and hydrophobic interactions. Those findings suggest an interaction between SARS-CoV-2 proteins and resin composites.
CONCLUSION
SARS-CoV-2 proteins show affinity to non-polymerised and polymerised resin composite chains.
Core Tip: The severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) may interact with monomers of resin composites; triethylene glycol dimethacrylate has the smallest affinity with SARS-CoV-2 among monomers; bisphenol-A glycol dimethacrylate and bisphenol-A ethoxylated dimethacrylate show a remarkable affinity mainly with papain-like protease.
