The Structures and Binding Modes of Small-Molecule Inhibitors of <i>Pseudomonas aeruginosa</i> Elastase LasB
Elastase B (LasB) is a zinc metalloprotease and a crucial virulence factor of <i>Pseudomonas aeruginosa</i>. As the need for new strategies to fight antimicrobial resistance (AMR) constantly rises, this protein has become a key target in the development of novel antivirulence agents. The...
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| Main Authors: | , , , |
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| Format: | Book |
| Published: |
MDPI AG,
2022-08-01T00:00:00Z.
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| Online Access: | Connect to this object online. |
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| Summary: | Elastase B (LasB) is a zinc metalloprotease and a crucial virulence factor of <i>Pseudomonas aeruginosa</i>. As the need for new strategies to fight antimicrobial resistance (AMR) constantly rises, this protein has become a key target in the development of novel antivirulence agents. The extensive knowledge of the structure of its active site, containing two subpockets and a zinc atom, led to various structure-based medicinal chemistry programs and the optimization of several chemical classes of inhibitors. This review provides a brief reminder of the structure of the active site and a summary of the disclosed <i>P. aeruginosa</i> LasB inhibitors. We specifically focused on the analysis of their binding modes with a detailed representation of them, hence giving an overview of the strategies aiming at targeting LasB by small molecules. |
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| Item Description: | 10.3390/antibiotics11081060 2079-6382 |