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- W2073236304 abstract "According to a primary structure proposed for an antibiotic peptide, gratisin, four peptides containing respectively partial sequences, L-Phe–L-Pro–L-Tyr, D-Phe–L-Pro–L-Tyr, L-Phe–L-Pro–D-Tyr, and D-Phe–L-Pro–D-Tyr, were synthesized by a liquid phase method. Among them, cyclo(–L-Val–L-Orn–L-Leu–D-Phe–L-Pro–D-Tyr–)2 showed the strongest activity against the Gram-positive microorganisms tested. The activity toward Bacillus subtilis was similar to that of gramicidin S. Therefore, it is quite possible that natural gratisin is identical to this peptide. To facilitate a further investigation of the structure-activity relationship, four additional analogs were prepared. The results of their antibiotic activities showed that an interchange of D-Phe residues with D-Tyr residues caused the decrease of activity, and that the hydroxyl group of D-Tyr residues had no important role in this activity. The peptides possessing partial sequences, D-Phe–D-Tyr–L-Pro and L-Pro–D-Phe–D-Phe, exhibited strong activity. These fact..." @default.
- W2073236304 created "2016-06-24" @default.
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- W2073236304 date "1984-11-01" @default.
- W2073236304 modified "2023-10-18" @default.
- W2073236304 title "Studies on Peptide Antibiotic “Gratisin”" @default.
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- W2073236304 doi "https://doi.org/10.1246/bcsj.57.3210" @default.
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