Phage display-derived inhibitor of the essential cell wall biosynthesis enzyme MurF.

ABSTRACT:

Background

To develop antibacterial agents having novel modes of action against bacterial cell wall biosynthesis, we targeted the essential MurF enzyme of the antibiotic resistant pathogen Pseudomonas aeruginosa. MurF catalyzes the formation of a peptide bond between D-Alanyl-D-Alanine (D-Ala-D-Ala) and the cell wall precursor uridine 5'-diphosphoryl N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-diaminopimelic acid (UDP-MurNAc-Ala-Glu-meso-A2pm) with the concomitant hydrolysis of ATP to ADP and inorganic phosphate, yielding UDP-N-acetylmuramyl-pentapeptide. As MurF acts on a dipeptide, we exploited a phage display approach to identify peptide ligands having high binding affinities for the enzyme.

Results

Screening of a phage display 12-mer library using purified P. aeruginosa Mu

SUBMITTER: Paradis-Bleau C 

PROVIDER: S-EPMC2626591 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature