Probing the binding site of curcumin in Escherichia coli and Bacillus subtilis FtsZ--a structural insight to unveil antibacterial activity of curcumin
| Autor: | Nilanjan Roy, Niraj Modi, Dulal Panda, Simranjeet Kaur |
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| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular Protein Conformation Bacillus subtilis medicine.disease_cause physiological processes Cd Binding Analysis chemistry.chemical_compound Tubulin Antibiotics Drug Discovery Cytoskeleton Antibacterial agent Ring biology Chemistry General Medicine Mep Ftsz Anti-Bacterial Agents Algorithm Biochemistry Flexible Docking biological phenomena cell phenomena and immunity Bacterial-Cell-Division Curcumin Static Electricity macromolecular substances Discovery Bacterial Proteins medicine Escherichia coli B. Subtilis Binding site FtsZ Protein Ftsz Pharmacology Binding Sites Sequence Homology Amino Acid Inhibitors Organic Chemistry Cytoskeleton Proteins biology.organism_classification Cytoskeletal Proteins Docking (molecular) Scoring Function biology.protein bacteria |
| Zdroj: | European journal of medicinal chemistry. 45(9) |
| ISSN: | 1768-3254 |
| Popis: | The cytoskeletal protein, FtsZ plays a pivotal role in prokaryotic cell division and is present in majority of the bacterial species. In recent years, inhibitors of FtsZ have been identified that may function as lead compounds for the development of novel antimicrobials. It has been found that curcumin, the main bioactive component of Curcuma longa, inhibits Bacillus subtilis and Escherichia coil growth by inhibiting FtsZ assembly. Though it is experimentally established that curcumin inhibits FtsZ polymerization, the binding site of curcumin in FtsZ is not known. In this study, interaction of curcumin with catalytic core domain of E. coli and B. subtilis FtsZ was investigated using computational docking. (C) 2010 Elsevier Masson SAS. . |
| Databáze: | OpenAIRE |
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