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Amide bioisosteric replacement in the design and synthesis of quorum sensing modulators.
- Source :
-
European journal of medicinal chemistry [Eur J Med Chem] 2024 Jul 05; Vol. 273, pp. 116525. Date of Electronic Publication: 2024 May 21. - Publication Year :
- 2024
-
Abstract
- The prevention or control of bacterial infections requires continuous search for novel approaches among which bacterial quorum sensing inhibition is considered as a complementary antibacterial strategy. Quorum sensing, used by many different bacteria, functions through a cell-to-cell communication mechanism relying on chemical signals, referred to as autoinducers, such as N-acyl homoserine lactones (AHLs) which are the most common chemical signals in this system. Designing analogs of these autoinducers is one of the possible ways to interfere with quorum sensing. Since bioisosteres are powerful tools in medicinal chemistry, targeting analogs of AHLs or other signal molecules and mimics of known QS modulators built on amide bond bioisosteres is a relevant strategy in molecular design and synthetic routes. This review highlights the application of amide bond bioisosteric replacement in the design and synthesis of novel quorum sensing inhibitors.<br />Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.<br /> (Copyright © 2024 The Authors. Published by Elsevier Masson SAS.. All rights reserved.)
- Subjects :
- Acyl-Butyrolactones pharmacology
Acyl-Butyrolactones chemistry
Acyl-Butyrolactones chemical synthesis
Acyl-Butyrolactones metabolism
Molecular Structure
Bacteria drug effects
Quorum Sensing drug effects
Drug Design
Amides chemistry
Amides pharmacology
Amides chemical synthesis
Anti-Bacterial Agents pharmacology
Anti-Bacterial Agents chemical synthesis
Anti-Bacterial Agents chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1768-3254
- Volume :
- 273
- Database :
- MEDLINE
- Journal :
- European journal of medicinal chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 38801798
- Full Text :
- https://doi.org/10.1016/j.ejmech.2024.116525