Reference

Studies of peptide antibiotics

Studies of peptide antibiotics. XLIV. Syntheses and biological activities of gramicidin S analogs containing w-hydroxy-L-norvaline or glycine. Yonezawa, Hiroo; Okamoto, Kouji; Kaneda, Makoto; Tominaga, Naotomo; Izumiya, Nobuo (Fac. Sci., Kagoshima Univ., Kagoshima 890, Japan).There are some reagents with their cas registry numbers 1068-90-2 and 54314-84-0 are used in this study. Int. J. Pept. Protein Res., 22(5), 573-81 (English) 1983. CODEN: IJPPC3. ISSN: 0367-8377. DOCUMENT TYPE: Journal CA Section: 10 (Microbial Biochemistry) Section cross-reference(s): 34 The antibiotic gramicidin S (GS) has the structure of cyclo(-L-Val1-L-Orn2-L-Leu3-D-Phe4-L-Pro5-L-Val1'-L-Orn2'-L-Leu3'-D-Phe4'-L -Pro5'-) and is basic in character. Five GS analogs including [Gly1,1']-GS and the neutral [L-Hnv2,2']-GS (Hnv represents d-hydroxynorvaline) were synthesized by the solid-phase method to evaluate the role of L-Val1,1' and L-Orn2,2' residues in GS. The hybrid analogs ([Gly1]-GS and [L-Hnv2]-GS) and [D-Tyr4,4']-GS showed high antibacterial activities, whereas [Gly1,1']-GS and [L-Hnv2,2']-GS possessed no activity. Inhibitory effects by these analogs for the adsorption of 14C-labeled GS on cells of bacteria sensitive to GS were detd. The structure-activity relationship of GS is discussed on the basis of the results on these GS analogs. .