scholarly journals Molecular docking studies of gyrase inhibitors: weighing earlier screening bedrock

2021 ◽  
Vol 9 (1) ◽  
Author(s):  
H. S. Santosh Kumar ◽  
S. Ravi Kumar ◽  
N. Naveen Kumar ◽  
S. Ajith
Keyword(s):  
Molecular Docking ◽  
Docking Studies ◽  
Molecular Docking Studies ◽  
Gyrase Inhibitors

scholarly journals Experimental and Molecular Docking Studies of Cyclic Diphenyl Phosphonates as DNA Gyrase Inhibitors for Fluoroquinolone-Resistant Pathogens

Antibiotics ◽  
2022 ◽  
Vol 11 (1) ◽  
pp. 53
Author(s):  
Neveen M. Saleh ◽  
Yasmine S. Moemen ◽  
Sara H. Mohamed ◽  
Ghady Fathy ◽  
Abdullah A. S. Ahmed ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Dna Gyrase ◽  
Docking Study ◽  
Dna Supercoiling ◽  
Docking Studies ◽  
Clinical Isolates ◽  
Detectable Effect ◽  
Topoisomerase Iv ◽  
Molecular Docking Studies ◽  
Gyrase Inhibitors

DNA gyrase and topoisomerase IV are proven to be validated targets in the design of novel antibacterial drugs. In this study, we report the antibacterial evaluation and molecular docking studies of previously synthesized two series of cyclic diphenylphosphonates (1a–e and 2a–e) as DNA gyrase inhibitors. The synthesized compounds were screened for their activity (antibacterial and DNA gyrase inhibition) against ciprofloxacin-resistant E.coli and Klebsiella pneumoniae clinical isolates having mutations (deletion and substitution) in QRDR region of DNA gyrase. The target compound (2a) that exhibited the most potent activity against ciprofloxacin Gram-negative clinical isolates was selected to screen its inhibitory activity against DNA gyrase displayed IC50 of 12.03 µM. In addition, a docking study was performed with inhibitor (2a), to illustrate its binding mode in the active site of DNA gyrase and the results were compatible with the observed inhibitory potency. Furthermore, the docking study revealed that the binding of inhibitor (2a) to DNA gyrase is mediated and modulated by divalent Mg2+ at good binding energy (–9.08 Kcal/mol). Moreover, structure-activity relationships (SARs) demonstrated that the combination of hydrazinyl moiety in conjunction with the cyclic diphenylphosphonate based scaffold resulted in an optimized molecule that inhibited the bacterial DNA gyrase by its detectable effect in vitro on gyrase-catalyzed DNA supercoiling activity.

Novel 2-arylbenzothiazole DNA gyrase inhibitors: Synthesis, antimicrobial evaluation, QSAR and molecular docking studies

2019 ◽  
Vol 93 ◽  
pp. 103373 ◽  
Author(s):  
Iman A.Y. Ghannam ◽  
Eman A. Abd El-Meguid ◽  
Islam H. Ali ◽  
Donia H. Sheir ◽  
Ahmed M. El Kerdawy
Keyword(s):  
Molecular Docking ◽  
Dna Gyrase ◽  
Docking Studies ◽  
Molecular Docking Studies ◽  
Antimicrobial Evaluation ◽  
Gyrase Inhibitors

Homology Modeling of Mus Musculus CDK5 and Molecular Docking Studies with Flavonoids

2017 ◽  
Vol 9 (6) ◽  
Author(s):  
Sowmya Suri ◽  
Rumana Waseem ◽  
Seshagiri Bandi ◽  
Sania Shaik
Keyword(s):  
Molecular Docking ◽  
3D Model ◽  
Structural Features ◽  
Docking Studies ◽  
Amino Acid Residues ◽  
Cyclin Dependent Kinase ◽  
Ligand Complex ◽  
Ligand Interaction ◽  
Molecular Docking Studies ◽  
Cyclin Dependent Kinase 5

A 3D model of Cyclin-dependent kinase 5 (CDK5) (Accession Number: Q543f6) is generated based on crystal structure of P. falciparum PFPK5-indirubin-5-sulphonate ligand complex (PDB ID: 1V0O) at 2.30 Å resolution was used as template. Protein-ligand interaction studies were performed with flavonoids to explore structural features and binding mechanism of flavonoids as CDK5 (Cyclin-dependent kinase 5) inhibitors. The modelled structure was selected on the basis of least modeler objective function. The model was validated by PROCHECK. The predicted 3D model is reliable with 93.0% of amino acid residues in core region of the Ramachandran plot. Molecular docking studies with flavonoids viz., Diosmetin, Eriodictyol, Fortuneletin, Apigenin, Ayanin, Baicalein, Chrysoeriol and Chrysosplenol-D with modelled protein indicate that Diosmetin is the best inhibitor containing docking score of -8.23 kcal/mol. Cys83, Lys89, Asp84. The compound Diosmetin shows interactions with Cys83, Lys89, and Asp84.

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