Structural dynamics and anti-biofilm screening of novel imidazole derivative to explore their anti-biofilm inhibition mechanism against Pseudomonas Aeruginosa

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dc.contributor.authorMehmood, Shahab
dc.contributor.authorHussain, Mumtaz
dc.contributor.authorBux, Khair
dc.contributor.authorHussain, Zahid
dc.contributor.authorRaza Shah, Muhammad
dc.contributor.authorAli Jakhrani, Mushtaque
dc.contributor.authorAli Channar, Pervaiz
dc.contributor.authorBegum, Irshad
dc.contributor.authorSaboor, Rukhsana
dc.contributor.authorYıldız, Cem B.
dc.contributor.authorAli, Kashif
dc.contributor.authorHerwig, Ralf
dc.date.accessioned2024-07-22T08:15:49Z
dc.date.available2024-07-22T08:15:49Z
dc.date.issued2024
dc.departmentTeknik Bilimler Meslek Yüksekokulu
dc.description.abstractThe biofilm formation is still prevalent mechanism of developing the drug resistance in the Pseudomonas aeruginosa, gram-negative bacteria, known for its major role in nosocomial, ventilator-associated pneumonia (VAP), lung infections and catheter-associated urinary tract infections. As best of our knowledge, current study first time reports the most potent inhibitors of LasR, a transcriptional activator of biofilm and virulence regulating genes in, Pseudomonas aeruginosa LasR, utilizing newly functionalized imidazoles (5a-d), synthesized via 1,3-dipolar cycloaddition using click approach. The synthesized ligands were characterized through Mass Spectrometry and 1H NMR. The binding potency and mode of biding of ligands. Quantum Mechanical(QM) methods were utilized to investigate the electronic basis, HOMO/LUMO and dipole moment of the geometry of the ligands for their binding potency. Dynamics cross correlation matrix (DCCMs) and protein surface analysis were further utilized to explore the structural dynamics of the protein. Free energy of binding of ligands and protein were further estimated using Molecular Mechanical Energies with the Poisson–Boltzmann surface area (MMPBSA) method. Molecular Docking studies revealed significant negative binding energies (5a ? 10.33, 5b ?10.09, 5c ? 10.11, and 5d ?8.33 KJ/mol). HOMO/LUMO and potential energy surface map estimation showed the ligands(5a) with lower energy gaps and larger dipole moments had relatively larger binding potency. The significant change in the structural dynamics of LasR protein due to complex formation with newlyfunctionalized imidazoles ligands.
dc.identifier.doi10.1080/07391102.2024.2317983
dc.identifier.issn0739-1102
dc.identifier.scopusqualityQ1
dc.identifier.urihttps:/dx.doi.org/10.1080/07391102.2024.2317983
dc.identifier.urihttps://hdl.handle.net/20.500.12451/12190
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherTaylor and Francis Ltd.
dc.relation.ispartofJournal of Biomolecular Structure and Dynamics
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectBiofil
dc.subjectMolecular Dynamics
dc.subjectMulti Drug Resistance
dc.subjectSimulations
dc.titleStructural dynamics and anti-biofilm screening of novel imidazole derivative to explore their anti-biofilm inhibition mechanism against Pseudomonas Aeruginosa
dc.typeArticle

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