DMAP-catalysed synthesis, antibacterial activity evaluation, cytotoxicity and docking studies of some heterocyclic molecules bearing sulfonamide moiety
By: Naaz Farha
.
Contributor(s): Srivastava, Ritika.
Publisher: New Delhi CSIR 2022Edition: Vol.61(9).Description: 951-960p.Subject(s): GENERAL CHEMISTRYOnline resources: Click here
In:
Indian journal of chemistry (Section B)Summary: DMAP has been shown to be a highly efficient nucleophilic catalyst when compared to triethylamine and pyridine using acetonitrile as solvent for the synthesis of a series of novel N- heterocyclic sulfonamide derivatives. The influence of the reaction parameters, like choice of solvent, catalyst, amount of catalyst and reaction time on product yield has been studied. Antibacterial screening involving a range of sulfonamide analogues as new peptide deformylase (PDF) inhibitors have been focused. The molecules show significant antibacterial activity (MIC value 6.2 − 3.1 µg/mL) against B. subtilis, S. pyrogenes, P. vulgaris and P. mirabilis. Potential in silico docking studies have been in conjugation with in vitro antibacterial results. Molecular docking of all compounds with PDF enzyme (PDB code: 1G2A) explain how certain moieties play significant roles in increasing the binding interactions and stabilizing the protein-ligand complexes. The compounds also have confirmed low extent of cytotoxicity when tested on HEL and HeLa cell lines.
| Item type | Current location | Call number | Status | Date due | Barcode | Item holds |
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Articles Abstract Database
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School of Pharmacy Archieval Section | Not for loan | 2023-0801 |
DMAP has been shown to be a highly efficient nucleophilic catalyst when compared to triethylamine and pyridine using acetonitrile as solvent for the synthesis of a series of novel N- heterocyclic sulfonamide derivatives. The influence of the reaction parameters, like choice of solvent, catalyst, amount of catalyst and reaction time on product yield has been studied. Antibacterial screening involving a range of sulfonamide analogues as new peptide deformylase (PDF) inhibitors have been focused. The molecules show significant antibacterial activity (MIC value 6.2 − 3.1 µg/mL) against B. subtilis, S. pyrogenes, P. vulgaris and P. mirabilis. Potential in silico docking studies have been in conjugation with in vitro antibacterial results. Molecular docking of all compounds with PDF enzyme (PDB code: 1G2A) explain how certain moieties play significant roles in increasing the binding interactions and stabilizing the protein-ligand complexes. The compounds also have confirmed low extent of cytotoxicity when tested on HEL and HeLa cell lines.
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