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Discovery of novel bacterial elongation condensing enzyme inhibitors by virtual screening.


ABSTRACT: The elongation condensing enzymes in the bacterial fatty acid biosynthesis pathway represent desirable targets for the design of novel, broad-spectrum antimicrobial agents. A series of substituted benzoxazolinones was identified in this study as a novel class of elongation condensing enzyme (FabB and FabF) inhibitors using a two-step virtual screening approach. Structure activity relationships were developed around the benzoxazolinone scaffold showing that N-substituted benzoxazolinones were most active. The benzoxazolinone scaffold has high chemical tractability making this chemotype suitable for further development of bacterial fatty acid synthesis inhibitors.

SUBMITTER: Zheng Z 

PROVIDER: S-EPMC4425204 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature

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Discovery of novel bacterial elongation condensing enzyme inhibitors by virtual screening.

Zheng Zhong Z   Parsons Joshua B JB   Tangallapally Rajendra R   Zhang Weixing W   Rock Charles O CO   Lee Richard E RE  

Bioorganic & medicinal chemistry letters 20140402 11


The elongation condensing enzymes in the bacterial fatty acid biosynthesis pathway represent desirable targets for the design of novel, broad-spectrum antimicrobial agents. A series of substituted benzoxazolinones was identified in this study as a novel class of elongation condensing enzyme (FabB and FabF) inhibitors using a two-step virtual screening approach. Structure activity relationships were developed around the benzoxazolinone scaffold showing that N-substituted benzoxazolinones were mos  ...[more]

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