Modeling of the adsorption of a protein-fragment on kaolinite with potential antiviral activityShow others and affiliations
2020 (English)In: Applied Clay Science, ISSN 0169-1317, E-ISSN 1872-9053, Vol. 199, article id 105865Article in journal (Refereed) Published
Abstract [en]
This work aimed at studying the potentiality of interactions between kaolinite surfaces and a protein-fragment (350–370 amino acid units) extracted from the glycoprotein E1 in the transmembrane domain (TMD) of hepatitis C virus capsid. A computational work was performed for locating the potential electrostatic interaction sites between kaolinite aluminol and siloxane surfaces and the residues of this protein-fragment ligand, monitoring the possible conformational changes. This hydrated neutralized kaolinite/protein-fragment system was simulated by means of molecular modeling based on atomistic force fields based on empirical interatomic potentials and molecular dynamic (MD) simulations. The MD calculations indicated that the studied protein-fragment interacted with the kaolinite surfaces with an exothermic process and structural distortions were observed, particularly with the hydrophilic aluminol surface by favorable adsorption energy. The viral units isolation or trapping by the adsorption on the kaolinite nanoparticles producing structural distortion of the peptide ligands could lead to the blockage of the entry on the receptor and hence a lack of viral activity would be produced. Therefore, these findings with the proposed insights could be an useful information for the next experimental and development studies in the area of discovering inhibitors of the global challenged hepatitis and other pathogenic viruses based on the phyllosilicate surface activity. These MD studies can be extended to other viruses like the COVID-19 interacting with silicate minerals surfaces.
Place, publisher, year, edition, pages
Elsevier, 2020. Vol. 199, article id 105865
Keywords [en]
Hepatitis C virus, Kaolinite, Molecular dynamics, Hydration, Adsorption, Virus sorption on minerals, Transmembrane domain, Glycoprotein E1
National Category
Aerospace Engineering
Research subject
Atmospheric science
Identifiers
URN: urn:nbn:se:ltu:diva-81146DOI: 10.1016/j.clay.2020.105865ISI: 000598135600002PubMedID: 33078035Scopus ID: 2-s2.0-85092444407OAI: oai:DiVA.org:ltu-81146DiVA, id: diva2:1476825
Note
Validerad;2020;Nivå 2;2020-10-15 (alebob)
2020-10-152020-10-152021-01-14Bibliographically approved