Chemical modification of erythromycins. I. Synthesis and antibacterial activity of 6-O-methylerythromycins A.

Morimoto, Shigeo; Takahashi, Yōko; Watanabe, Yoshiaki; Omura, Sadafumi

doi:10.7164/antibiotics.37.187

Cited by 215 publications

(78 citation statements)

References 16 publications

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“…Clarithromycin (CLA; chemical name-6-O-methylerythromycin, 1) [8] is a macrolide antibiotic that is widely used in clinical medicine. Macrolide antibiotics such as CLA specifically bind to the 50S subunit of the bacterial ribosome thereby interfering with protein biosynthesis [9].…”

Section: Introductionmentioning

confidence: 99%

Identification of Antibiotic Clarithromycin Binding Peptide Displayed by T7 Phage Particles

et al. 2006

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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 2.1ϫ10 Ϫ3 M. The dissociation constants of other macrolide antibiotics, erythromycin, roxithromycin, azithromycin and josamycin were also determined to be 5.4ϫ10 Ϫ3 M, 6.2ϫ10 Ϫ5 M, 1.1 M and 3.4ϫ10 Ϫ2 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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Section: Introductionmentioning

confidence: 99%

Identification of Antibiotic Clarithromycin Binding Peptide Displayed by T7 Phage Particles

et al. 2006

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“…The organic phase was washed with water, dried over MgSO 4 , filtered and concentrated in vacuo. The resulting residue was purified by preparative thin-layer chromatography (CHCl 3 /CH 3 OH/28% aq NH 4 …”

Section: Experimental Procedures Generalmentioning

confidence: 99%

“…Lincosamide antibiotics are protein synthesis inhibitors 3 that act on 50S ribosome in a similar way to macrolide antibiotics such as clarithromycin. 4 However, CLDM shows almost no antibacterial activity against resistant pathogens such as Streptococcus pneumoniae and Streptococcus pyogenes with erm gene as shown in Table 1. Moreover, major macrolides, clarithromycin and azithromycin, 5 are also not active against those pathogens with erm gene.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and antibacterial activity of novel lincomycin derivatives. II. Exploring (7S)-7-(5-aryl-1,3,4-thiadiazol-2-yl-thio)-7-deoxylincomycin derivatives

et al. 2016

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The synthesis and antibacterial activity of (7S)-7-(5-aryl-1,3,4-thiadiazol-2-yl-thio)-7-deoxylincomycin derivatives are described. These derivatives were mainly prepared by the Mitsunobu reaction of 2,3,4-tris-O-(trimethylsilyl)lincomycin and the corresponding thiols. Exploring structure-activity relationships of the substituent at the 5 position of a thiadiazole ring revealed that compounds with the ortho substituted phenyl group showed improved antibacterial activities against Streptococcus pneumoniae and Streptococcus pyogenes with erm gene compared with the reported compound (1) that had an unsubstituted benzene ring.

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“…Launched in 1990 by Abbott Laboratories, clarithromycin A (CLA: synonym of 6-O-methylerythromycin, 1) [1] is a macrolide antibiotic that is commonly used to treat a variety of human bacterial infections. Macrolide antibiotics, represented by erythromycin A (ERY, 2) and its structural homologues, specifically bind to the bacterial 50S ribosomal subunit resulting in the inhibition of bacterial protein biosynthesis [2].…”

Section: Introductionmentioning

confidence: 99%

Identification of Macrolide Antibiotic-binding Human_p8 Protein

et al. 2008

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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.

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Chemical modification of erythromycins. I. Synthesis and antibacterial activity of 6-O-methylerythromycins A.

Cited by 215 publications

References 16 publications

Identification of Antibiotic Clarithromycin Binding Peptide Displayed by T7 Phage Particles

Identification of Antibiotic Clarithromycin Binding Peptide Displayed by T7 Phage Particles

Synthesis and antibacterial activity of novel lincomycin derivatives. II. Exploring (7S)-7-(5-aryl-1,3,4-thiadiazol-2-yl-thio)-7-deoxylincomycin derivatives

Identification of Macrolide Antibiotic-binding Human_p8 Protein

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