Journal: Journal of Medicinal Chemistry

Article Title: Development of Fragment-Based Inhibitors of the Bacterial Deacetylase LpxC with Low Nanomolar Activity

doi: 10.1021/acs.jmedchem.4c01262

Figure Lengend Snippet: (A) LpxC-catalyzed deacetylation of UDP-3- O -[( R )-3-hydroxymyristoyl]- N -acetylglucosamine ( 1 ). (B) Molecular surface (colored according to the hydrophobicity, polar regions are colored magenta, hydrophobic regions are colored green) of E. coli LpxC near the deacetylated natural product 2 (PDB ID: 4MDT ). UDP-3- O -[( R )-3-hydroxymyristoyl]-glucosamine ( 2 ) is shown as a cyan colored ball and stick model.

Article Snippet: The disc diffusion assays against E. coli TOP10 (Thermo Fisher, Waltham, USA), E. coli ATCC 35218, K. pneumoniae ATCC 700603, and P. aeruginosa ATCC 27853 were performed as follows: the bacteria were grown overnight on a Columbia blood agar plate (Oxoid, Basingstoke, UK), and one colony was suspended in sterile saline to yield a suspension of 0.5 McFarland standard.

Techniques:

Journal: Journal of Medicinal Chemistry

Article Title: Development of Fragment-Based Inhibitors of the Bacterial Deacetylase LpxC with Low Nanomolar Activity

doi: 10.1021/acs.jmedchem.4c01262

Figure Lengend Snippet: Structures of the described LpxC inhibitors targeting the enzyme’s UDP-binding site. Reported inhibitory activities toward E. coli LpxC ( Ec LpxC) and P. aeruginosa LpxC ( Pa LpxC) are given. −

Article Snippet: The disc diffusion assays against E. coli TOP10 (Thermo Fisher, Waltham, USA), E. coli ATCC 35218, K. pneumoniae ATCC 700603, and P. aeruginosa ATCC 27853 were performed as follows: the bacteria were grown overnight on a Columbia blood agar plate (Oxoid, Basingstoke, UK), and one colony was suspended in sterile saline to yield a suspension of 0.5 McFarland standard.

Techniques: Binding Assay