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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.


Tetsuro Morimura, Mio Hashiba, Hiroshi Kameda, Mihoko Takami, Hirokazu Takahama, Masahiko Ohshige, Fumio Sugawara. Identification of macrolide antibiotic-binding Human_p8 protein. The Journal of antibiotics. 2008 May;61(5):291-6

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PMID: 18653994

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