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  • Title: Identification of antibiotic clarithromycin binding peptide displayed by T7 phage particles.
    Author: Morimura T, Noda N, Kato Y, Watanabe T, Saitoh T, Yamazaki T, Takada K, Aoki S, Ohta K, Ohshige M, Sakaguchi K, Sugawara F.
    Journal: J Antibiot (Tokyo); 2006 Oct; 59(10):625-32. PubMed ID: 17191677.
    Abstract:
    Peptide libraries displayed by T7 phage, which contain random cDNA fragments insets, were screened for their ability to bind to a biotinylated derivative of clarithromycin. Phage particles bound to an immobilized derivative of the antibiotic were isolated and the inserted cDNA was amplified and sequenced. A common selected peptide sequence, composed of 19 amino acids, was obtained and a synthetic peptide with this sequence was produced. Surface plasmon resonance experiments showed that the synthetic peptide immobilized on a sensor chip bound to clarithromycin and the dissociation constant was determined to be 2.1 x 10(-3) M. The dissociation constants of other macrolide antibiotics, erythromycin, roxithromycin, azithromycin and josamycin were also determined to be 5.4 x 10(-3) M, 6.2 x 10(-5) M, 1.1 M and 3.4 x 10(-2) M, respectively. These results indicated that T7 phage display method might be useful to determine relatively weak interactions between small molecule drugs and the selected peptides which could represent a possible binding site conserved in binding proteins.
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