The inhibition of LpxC, an enzyme involved in the first committed step of the biosynthesis of Lipid A, is attractive for the development of novel antibacterial treatments. Through analysis of its crystal structure, it was determined that LpxC contains three key regions in its active site: a zinc binding motif, a hydrophobic passage, and a polar region. The synthesis of derivatives containing the nucleoside and zinc binding motif have been accomplished. Using CuAAC, a triazole linker was used to couple a nucleoside and zinc binding motif in order to yield the final potential inhibitors. Derivatives without the nucleoside have been designed and synthesized in order to examine the importance of the nucleoside in binding. The synthesis and chemical and enzymatic stability of these compounds will be discussed.<br/>

Synthesis and analysis of propargylglycine-based derivatives as potential inhibitors of LpxC

253rd National Meeting (2017)

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