N-(naphthalen-1-yl(phenyl)carbamothioyl)-3-nitrobenzamide against Methicillin-resistant Staphylococcus aureus (MRSA) isolates: Thermal kinetics, theoretical and molecular docking studies

Kutlu E., YILDIRIM K., Emen F. M., Ali M. A., Licina M., ÇOBAN A. Y., ...Daha Fazla

Journal of Molecular Structure, cilt.1330, 2025 (SCI-Expanded) identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 1330
  • Basım Tarihi: 2025
  • Doi Numarası: 10.1016/j.molstruc.2025.141428
  • Dergi Adı: Journal of Molecular Structure
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Chemical Abstracts Core, Chimica, Compendex, INSPEC
  • Anahtar Kelimeler: 3-nitrobenzamide, Aroylthiouurea, Methicillin-resistant staphylococcus aureus (MRSA), Molecular docking, Termal analysis
  • Akdeniz Üniversitesi Adresli: Evet

Özet

In this study, the thiourea derivative N-(naphthalen-1-yl(phenyl)carbamothioyl)-3-nitrobenzamide ligand (HL) was synthesized and structurally characterized using FT-IR and 1H NMR spectrometers. The thermal properties of HL were analyzed using a Thermal Gravimetry/Differential Thermal Gravimetry/Differential Thermal Analysis (TG/DTG/DTA) system. Kinetic parameters were calculated using the Flynn–Wall–Ozawa (FWO) and Kissinger–Akahira–Sunose (KAS) methods, with activation energies (Ea ) determined as 170.71–87.92 kJ mole-1 (FWO) and 166.40–83.71 kJ mole-1 (KAS) for each decomposition stage. Quantum chemical calculations were conducted via Density Functional Theory (DFT) at the B3LYP/6–311G(d,p) level of theory using the Gaussian 09 program package. The antimicrobial efficacy of HL against Methicillin-resistant Staphylococcus aureus (MRSA) isolates was also investigated. Minimum inhibitory concentration (MIC) values were calculated as follows: ≤0.25 µg/mL for 7 isolates, 0.5 µg/mL for 30 isolates, 1 µg/mL for 57 isolates, 2 µg/mL for 28 isolates, 4 µg/mL for 7 isolates, 8 µg/mL for 11 isolates, 64 µg/mL for 3 isolates, 128 µg/mL for 1 isolate, and 256 µg/mL for 6 isolates. The variation in antimicrobial activity may be attributed to the resistance mechanisms of individual isolates. The high efficacy of HL, particularly against MRSA isolates, suggests its potential as a drug precursor for treating S. aureus-related infections. Molecular docking studies revealed binding scores with MRSA proteins (1MWR, 1MWS, 1MWT, 1VQQ, and 6H5O) ranging from -8.1 to -9.8 kcal/mole, further demonstrating HL's reactivity against MRSA proteins.