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Erythromycin-metal complexes: One-step synthesis, molecular docking analysis and antibacterial proficiency against pathogenic strains.
Egu, Samuel Attah; Abah, Lian Ojotule; Hussaini, Jumai Zainab; Onoja, Alexander David; Ali, Irfan; Habib, Atiya; Qureshi, Urooj; Idih, Sunday Okpanachi; Edegbo, Emmanuel; Achimugu, Lawrence; Omale, Aminu; Michael, Ojochide Charity; Adaji, Mohammed Umar; Omale, Jamila Audu.
Afiliación
  • Egu SA; Department of Pure and Industrial Chemistry, Kogi State University, Anyigba, Kogi State, Nigeria.
  • Abah LO; Genomics and Molecular Biology Training and Research Laboratory, Kogi State University, Anyigba, Kogi State, Nigeria.
  • Hussaini JZ; Department of Pure and Industrial Chemistry, Kogi State University, Anyigba, Kogi State, Nigeria.
  • Onoja AD; Department of Pure and Industrial Chemistry, Kogi State University, Anyigba, Kogi State, Nigeria.
  • Ali I; Department of Pure and Industrial Chemistry, Kogi State University, Anyigba, Kogi State, Nigeria.
  • Habib A; H. E. J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi, 75270, Pakistan.
  • Qureshi U; Dr. Panjwani Center for Molecular Medicine and Drug Research, International Center for Chemical and Biological Sciences, University of Karachi, Karachi, 75270, Pakistan.
  • Idih SO; Dr. Panjwani Center for Molecular Medicine and Drug Research, International Center for Chemical and Biological Sciences, University of Karachi, Karachi, 75270, Pakistan.
  • Edegbo E; Department of Pure and Industrial Chemistry, Kogi State University, Anyigba, Kogi State, Nigeria.
  • Achimugu L; Department of Microbiology, Kogi State University, Anyigba, Kogi, Nigeria.
  • Omale A; Department of Science Education, Kogi State University, Anyigba, Kogi, Nigeria.
  • Michael OC; Department of Pure and Industrial Chemistry, Kogi State University, Anyigba, Kogi State, Nigeria.
  • Adaji MU; Department of Pure and Industrial Chemistry, Kogi State University, Anyigba, Kogi State, Nigeria.
  • Omale JA; Department of Pure and Industrial Chemistry, Kogi State University, Anyigba, Kogi State, Nigeria.
Heliyon ; 10(16): e35536, 2024 Aug 30.
Article en En | MEDLINE | ID: mdl-39220992
ABSTRACT
The study focused on the extraction of free erythromycin from commercially manufactured tablets and the use of metal salts to synthesize erythromycin-metal complexes, specifically involving silver (Ag), nickel (Ni), cobalt (Co), and copper (Cu). The synthesis was confirmed through various methods, including elemental analysis, thermogravimetric analysis, Fourier-transform infrared (FTIR), and UV-visible spectroscopy. The microbiological investigation involved Salmonella typhi, Escherichia coli, Staphylococcus aureus, Bacillus cereus, Candida albicans, and Microsporum canis as test organisms. The NCCLS broth microdilution reference method was used to determine the minimum fungicidal concentration and minimum inhibitory concentration of the complexes. The synthesized complexes were highly effective against a variety of fungi and bacteria, with compound Ery-Cu having MIC as low as 1.56 mg/mL, Ery-Cu and Ery-Ni with MBCs of 6.25 mg/mL and Ery-Cu having MFC of 6.25 mg/mL. Dose-dependent inhibitory effects were found upon examination of the antimicrobial susceptibility of specific complexes (Cu, Ni, Co and Ag) at varying concentrations of 100, 50, 25 and 12.5 mm/mL. Antibiotic susceptibility testing revealed efficacy against the tested pathogens. The study suggests that the synthesis of erythromycin-metal complexes, coupled with their antibacterial effectiveness against a diverse spectrum of bacteria and fungi, as they showed promising inhibitory properties when tested against a range of test species (Bacillus cereus, Staphylococcus aureus, Escherichia coli, Salmonella typhi, Candida albicans, and Microsporum canis), could lead to the development of innovative antibacterial agents. Molecular docking simulations were used to examine the interactions between metal complexes with proteins filamentous temperature-sensitive protein Z and lanosterol 14α-demethylase. The study highlights the need for further exploration in pharmaceutical research.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Heliyon Año: 2024 Tipo del documento: Article País de afiliación: Nigeria Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Heliyon Año: 2024 Tipo del documento: Article País de afiliación: Nigeria Pais de publicación: Reino Unido