(E)-2,4-Dibromo-6-((2-phenoxyphenylimino)methyl)phenol: Crystal structure, antibacterial activity, and insights into DNA Gyrase B interactions
JOURNAL OF MOLECULAR STRUCTURE, cilt.1381, 2027 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 1381
- Basım Tarihi: 2027
- Doi Numarası: 10.1016/j.molstruc.2026.147586
- Dergi Adı: JOURNAL OF MOLECULAR STRUCTURE
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Chemical Abstracts Core, Chimica, Compendex, INSPEC, Academic Search Ultimate (EBSCO), Engineering Source (EBSCO)
- Ondokuz Mayıs Üniversitesi Adresli: Evet
Özet
A dibrominated Schiff base, (E)-2,4-dibromo-6-((2-phenoxyphenylimino)methyl)phenol (DiBr-POP), was synthesized, structurally characterized using FT-IR, UV-Vis, NMR, and single-crystal X-ray diffraction, and evaluated for its antimicrobial activity. Density functional theory (DFT) calculations were in good agreement with the experimental geometry and yielded a HOMO-LUMO energy gap of 3.71 eV, indicating moderate chemical reactivity and favorable electronic stability. DiBr-POP exhibited promising antimicrobial activity against Grampositive and Gram-negative bacteria and antifungal activity against Candida albicans; MIC values were as low as 4 mu g/mL against several bacterial strains, including Pseudomonas aeruginosa, against which the compound demonstrated bactericidal activity (MIC = MBC = 4 mu g/mL). To explore a possible antibacterial mechanism underlying the activity, molecular docking studies were performed using the ATPase domain of P. aeruginosa DNA gyrase B (PDB ID: 7PTG). Redocking of the native co-crystallized ligand (EBL2888) yielded a heavy-atom RMSD value of 1.67 & Aring;, indicating satisfactory agreement with the crystallographic binding mode. DiBr-POP displayed favorable binding to DNA gyrase B, with a binding energy of-7.44 kcal/mol and an estimated inhibition constant (Ki) of 3.54 & micro;M. ADME analysis predicted favorable gastrointestinal absorption and membrane permeability. Collectively, these findings highlight DiBr-POP as a structurally interesting compound with promising antibacterial activity and they warrant further studies to evaluate DNA gyrase B as a potential molecular target of DiBr-POP.