Identification of macrolide antibiotic-binding Human_p8 protein.

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Morimura T, Hashiba M, Kameda H, Takami M, Takahama H, Ohshige M, Sugawara F

Identification of macrolide antibiotic-binding Human_p8 protein.

J Antibiot (Tokyo). 2008 May;61(5):291-6. doi: 10.1038/ja.2008.41.

PubMed ID

18653994 [ View in PubMed

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Abstract

Clarithromycin is a macrolide antibiotic that is widely used in clinical medicine. Macrolide antibiotics such as clarithromycin specifically bind to the 50S subunit of the bacterial ribosome thereby interfering with protein biosynthesis. A selected peptide sequence from our former study, composed of 19 amino acids, which was isolated from a phage display library because of its ability to bind clarithromycin, displayed significant similarity to a portion of the human_p8 protein. The recombinant p8 protein binds to biotinylated-clarithromycin immobilized on a streptavidin-coated sensor chip and the dissociation constant was determined. The binding of recombinant p8 protein to double-stranded DNA was inhibited by biotinylated-clarithromycin, clarithromycin, erythromycin and azithromycin in gel mobility shift assay. Dechlorogriseofulvin, obtained from a natural product screening, also inhibited human p8 protein binding to DNA. This study illustrates the general utility of the phage display method in detecting protein-ligand interactions.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Clarithromycin	50S ribosomal protein L10	Protein	Shigella flexneri	Yes	Inhibitor	Details