Synthesis of Antibacterial Disulfide Derivatives and its Computational Molecular Docking Against Penicillin Binding Protein

2021 ◽  
Vol 11 (5) ◽  
pp. 618-634
Author(s):  
Sunil Kumar ◽  
Mukesh Choudhary ◽  
Gaurav Kumar ◽  
Raman K. Singh ◽  
Santosh Kumar
Keyword(s):  
Molecular Docking ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Computational Molecular Docking

scholarly journals Synthesis, molecular docking studies, and antimicrobial evaluation of pyrano[2, 3-c]pyrazole derivatives

2021 ◽  
pp. 309-328 ◽  
Author(s):  
Samy A. El-Assaly ◽  
Abd El-Hamid A. Ismail ◽  
Hamed Abdel Bary ◽  
Mohamed G. Abouelenein
Keyword(s):  
Molecular Docking ◽  
Binding Protein ◽  
Diethyl Malonate ◽  
Docking Study ◽  
Docking Studies ◽  
Penicillin Binding Protein ◽  
Molecular Docking Study ◽  
One Pot ◽  
Bacterial Action ◽  
Potential Mode

A sequence of pyrano[2, 3-c]pyrazoles was constructed through promoting an eco-friendly, green, and efficient approach. M1-M25 derivatives were developed by a base-catalyzed one-pot reaction involving application of hydrazine hydrate 96%, β-keto ester as ethyl acetoacetate or diethyl malonate, aryl/heteroaryl aldehyde or isatin, and enolizable active methylene compounds with isolation of unexpected compound M2. Further on, intramolecular cyclization of compounds M10, M13 with formic acid, acetic anhydride, and formamide leads to the corresponding pyrimidine derivatives M26-M31. Afterwards, the antimicrobial activity of the compounds was evaluated and fortunately, the vast majority of the compounds showed outstanding anti-bacterial results. Besides, the potential mode of action of the synthesized compounds was determined by employing a molecular-docking study against penicillin-binding protein implicated in anti-bacterial action. Compound M21 was one of the most promising anti-bacterial agents with potential binding affinity against the penicillin-binding protein. This study shed light on novel compounds for further antimicrobial drug development.

scholarly journals PenA, a penicillin-binding protein-type thioesterase specialized for small peptide cyclization

2021 ◽  
Author(s):  
Kenichi Matsuda ◽  
Kei Fujita ◽  
Toshiyuki Wakimoto
Keyword(s):  
Enzymatic Activity ◽  
Computational Model ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Small Peptide ◽  
Peptide Cyclization ◽  
Chain Lengths ◽  
Non Ribosomal Peptides

Abstract Penicillin binding protein-type thioesterases (PBP-type TEs) are a recently identified group of peptide cyclases that catalyze head-to-tail macrolactamization of non-ribosomal peptides. PenA, a new member of this group, is involved in the biosyntheses of cyclic pentapeptides. In this study, we demonstrated the enzymatic activity of PenA in vitro, and analyzed its substrate scope with a series of synthetic substrates. A comparison of the reaction profiles between PenA and SurE, a representative PBP-type TE, showed that PenA is more specialized for small peptide cyclization. A computational model provided a possible structural rationale for the altered specificity for substrate chain lengths.

Synthesis of novel alkylphosphonates as promising antimicrobial drugs: Computational molecular docking studies

2021 ◽  
pp. 1-9
Author(s):  
Nayab Rasool Shaik ◽  
Nagaraju Kerru ◽  
Venkataramaiah Chintha ◽  
Kavita Khatana ◽  
Divijendra Natha Reddy Sirigiri ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Docking Studies ◽  
Antimicrobial Drugs ◽  
Molecular Docking Studies ◽  
Computational Molecular Docking
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