Molecular Docking Simulations of Protoporphyrin IX, Chlorin e6, and
Methylene Blue for Target Proteins of Viruses Causing Skin Lesions:
Monkeypox and HSV

Israel      Lara-Vega; Armando      Vega-López

Note! Please note that this article is currently in the "Article in Press" stage and is not the final "Version of record". While it has been accepted, copy-edited, and formatted, however, it is still undergoing proofreading and corrections by the authors. Therefore, the text may still change before the final publication. Although "Articles in Press" may not have all bibliographic details available, the DOI and the year of online publication can still be used to cite them. The article title, DOI, publication year, and author(s) should all be included in the citation format. Once the final "Version of record" becomes available the "Article in Press" will be replaced by that.

Abstract

Background: The replication of monkeypox in the skin is critical to understanding its pathogenesis and spread. p37, a highly conserved 37 kDa peripheral membrane protein encoded by the F13L gene in Orthopoxvitidae is a validated target for anti-poxviral medication like tecovirimat, the first FDA-approved anti-poxviral drug that was approved in 2018. The detailed recognition mechanism of tecovirimat on p37 of monkeypox has not been fully clarified. As p37, HSV-1 gD and HSV-2 gD proteins of HSV are viral envelope glycoproteins identified as ligands for the human nectin-1 as a functional receptor of permissive cells. The use of non-damaging light for microbial inactivation (MI) has been documented for different virus like HSV, where photosensitizers (PSs) are used as lightresponsive agents which could generate antiviral responses primarily by oxidation. In addition, some PSs could elicit antiviral responses in a light-independent way by interacting within the viral-cell recognition sites.

Objective: This paper aims to evaluate the formation of complexes between the latest structural data available on the range of monkeypox and HSV-1/2 envelope proteins with the approved PSs protoporphyrin IX, chlorin e6, and methylene blue.

Methods: Ligands and receptors preparation, and molecular docking analyses were performed with Chimera and the Autodock Vina Software. Molecular docking and molecular dynamics simulation (MD) analyses for a 100 ns trajectory were also performed for the p37 – Methylene blue complex.

Results: PSs studies were found to form complexes into the patch regions of recognition between HSV-1/2 gD and human receptors, while MB was found to form a complex with the p37 protein into de pocket region where tecovirimat acts. MD simulation showed stability in the interaction of MB with the pocket region of the p37 protein.

Conclusion: The molecular mechanisms of potential dual antiviral activity for these complexes were clarified showing that MI with the use of these PSs could be further evaluated for viral skin lesions produced by monkeypox and HSV.

Keywords: photosensitizer, photodynamic therapy, tecovirimat, orthopoxvirus, herpes simplex, molecular docking, molecular dynamics

Rights & Permissions Print Cite

Journal Information

For Authors

For Editors

For Reviewers

Explore Articles

Open Access

Open Access Articles

For Visitors

DOI https://dx.doi.org/10.2174/0115701808247788230919172400	Print ISSN 1570-1808
Publisher Name Bentham Science Publisher	Online ISSN 1875-628X

Letters in Drug Design & Discovery

Molecular Docking Simulations of Protoporphyrin IX, Chlorin e6, and Methylene Blue for Target Proteins of Viruses Causing Skin Lesions: Monkeypox and HSV

Abstract

Related Journals

Related Books