MOLECULAR DOCKING STUDY ON THE INTERACTION OF CAFFEIC ACID, CAFFEIC ACID PHENETHYL ESTER (CAPE) AND GENISTEIN MOLECULES WITH SULFITE EFFLUX PUMP SSU1 AND SUBTILISIN-LIKE PROTEASE 1 PROTEINS
VIII. International Agricultural, Biological & Life Science Conference, İstanbul, Türkiye, 06-09 September 2026, İstanbul, Türkiye, 6 - 09 Eylül 2026, ss.459, (Özet Bildiri)
- Yayın Türü: Bildiri / Özet Bildiri
- Basıldığı Şehir: İstanbul
- Basıldığı Ülke: Türkiye
- Sayfa Sayıları: ss.459
- İstanbul Gelişim Üniversitesi Adresli: Evet
Özet
Dermatophytosis is the most common infection worldwide, affecting the stratum corneum of the skin, nails, and hair with a high recurrence rate. This fungal infection is caused by dermatophytes, which are filamentous fungi that can infect keratinized tissues in both animals and humans, particularly Trichophyton mentagrophytes, T. rubrum, T. tonsurans, Microsporum canis, Nannizzia gypsea, and Epidermophyton floccosum. Propolis is a resinous substance produced by honeybees and has been utilized in traditional medicine for centuries due to its numerous biological properties. Propolis resin contains a variety of phenolic compounds. In both humans and animals, these compounds demonstrate a variety of biological activities, including antibacterial, antifungal, antiviral effects. In our previous study, we evaluated the in vitro antifungal activity of a propolis extract collected from the Muğla region against M. canis and N. gypsea. We found that propolis effectively inhibited mycelial growth in all tested dermatophyte field isolates at every concentration assessed. In this study, we investigated the interaction between caffeic acid, caffeic acid phenethyl ester (CAPE), and genistein—major phenolic compounds in the propolis extract—and certain virulence-related factors of the M. canis and N. gypsea fungus species using molecular docking method. According to the data obtained, it was determined that the Sulfite efflux pump SSU1 virulence factor of M. canis showed a binding energy of -7.3 kcal/mol with genistein, -6.4 kcal/mol with CAPE, and -6.2 kcal/mol with caffeic acid. It was determined that the subtilisin-like protease 1 virulence factor of N. gypsea showed binding energies of -6.0 kcal/mol with genistein, -5.4 kcal/mol with caffeic acid, and -5.3 kcal/mol with CAPE. The findings suggest that caffeic acid, CAPE, and genistein molecules can show significant binding affinity to SSU1 and subtilisin-like protease 1 proteins and may be potential inhibitory molecules in M. canis and N. gypsea dermatophytosis cases.