title: Peptidyl-tRNA hydrolase screening combined with molecular docking reveals the antibiotic potential of Syzygium johnsonii bark extract.
abstract: With the rapid rise of antibiotic resistance in pathogenic bacteria, the need for new antibacterial agents is overwhelming. Herein we report the limited screening of tropical plant extracts for inhibitory activity against the essential enzyme peptidyl-tRNA hydrolase (Pth). Initial screening was conducted through an electrophoretic mobility assay and Northern blot detection. The ability of Pth to cleave the peptide-tRNA ester bond was assessed. The ethanol bark extract of Syzygium johnsonii showed strong inhibitory potential. Molecular docking studies point to Syzygium polyphenolics as the potential source of inhibition. This work is the forerunner of activity-directed isolation, purification, and structure elucidation of the inhibitory components from Syzygium johnsonii extracts and studies of compound interaction with Pth.
authors.affiliation: Department of Chemistry, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
authors.forename: Sarah M
authors.initials: SM
authors.lastname: Harris
authors.forename: Hana
authors.initials: H
authors.lastname: McFeeters
authors.forename: Ifedayo V
authors.initials: IV
authors.lastname: Ogungbe
authors.forename: Luis R
authors.initials: LR
authors.lastname: Cruz-Vera
authors.forename: William N
authors.initials: WN
authors.lastname: Setzer
authors.forename: Betsy R
authors.initials: BR
authors.lastname: Jackes
authors.forename: Robert L
authors.initials: RL
authors.lastname: McFeeters
mesh_terms: D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000494:pharmacology*; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D024301:Plant Bark / Q000737:chemistry*; D010936:Plant Extracts / Q000737:chemistry / Q000494:pharmacology*; D027842:Syzygium / Q000737:chemistry*
chemical_list: D000900:Anti-Bacterial Agents; D010936:Plant Extracts; D002265:Carboxylic Ester Hydrolases; C019674:aminoacyl-tRNA hydrolase