Cyanidin-3-O-rhamnoside: A promising inhibitor of the virulence protein subtilisin-like protease-1 in Microsporum gypseum

Bakrudeen Ali Ahmed Abdul

Department of Biochemistry, Research Development Cell (RDC), PRIST Deemed University, Thanjavur, Tamil Nadu, India.

Vijay Lobo

Department of Biochemistry, Research Development Cell (RDC), PRIST Deemed University, Thanjavur, Tamil Nadu, India.

Amjath Khan

Department of Biochemistry, Research Development Cell (RDC), PRIST Deemed University, Thanjavur, Tamil Nadu, India.

Subhashini Ramakrishnan

Department of Biotechnology, Dr.G.R.Damodaran college of Science, Coimbatore – 641014, Tamil Nadu, India.

Ramathilaga Ariyamuthu

Department of Biotechnology, Dr.G.R.Damodaran college of Science, Coimbatore – 641014, Tamil Nadu, India.

Balambigai Narayanasamy

Department of Biotechnology, Dr.G.R.Damodaran college of Science, Coimbatore – 641014, Tamil Nadu, India.

DOI: https://doi.org/10.14456/apst.2025.32

Keywords: Microsporum gypseum Subtilisin-like protease1 AlphaFold Cyanidin-3-O-rhamnoside docking MD simulation

Abstract

Microsporum gypseum, a keratinophilic fungus belonging to the dermatophyte group causes infections of the skin, hair, and nails in humans and animals, leading to conditions such as tinea capitis, tinea corporis, and tinea faciei. Virulence factors play a crucial role in the pathogenicity and subsequent host tissue damage. In dermatopytes, proteases are the primary virulence factors, which facilitate host invasion and utilization of the stratum corneum. Unlike most studies targeting the ergosterol biosynthesis pathway for the treatment of fungal infections, this research focuses on a major virulence enzyme, subtilisin-like protease (SUB-1), employing in silico evaluation of antifungal compounds against this enzyme. The three-dimensional structure of SUB-1 was retrieved from the AlphaFold database and evaluated using the prediction local distance difference test (pLDDT) scores and a Ramachandran plot. Active site residues were identified based on a literature review and using the webserver ConSurf. Structures of compounds were downloaded from the PubChem database, and the physicochemical properties were analyzed using the Swiss ADME database. Selected compounds were then docked with the SUB-1 by using Glide software, and molecular dynamics simulations were conducted using the Desmond module of Schrödinger for identifying the best-docked complex structure. The results revealed that cyanidin-3-O-rhamnoside exhibits potent activity against SUB-1, with a docking score of -9.4 kcal/mol, binding free energy of -55.23 kcal/mol, and interactions with the active site residues H190, N282, and H342. The efficiency of this compound in inhibiting the growth of M. gypseum needs to be validated further using experimental studies.

How to Cite

Ali Ahmed Abdul, B. ., Lobo, V. ., Khan, A. ., Ramakrishnan, S. ., Ariyamuthu , R. ., & Narayanasamy , B. . (2025). Cyanidin-3-O-rhamnoside: A promising inhibitor of the virulence protein subtilisin-like protease-1 in Microsporum gypseum. Asia-Pacific Journal of Science and Technology, 30(02), APST–30. https://doi.org/10.14456/apst.2025.32

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