The producer strain of the new antibiotic, lipiarmycin, is described. The colony morphology, the presence of globose sporangia bearing motile spores, the absence of aerial mycelium and the presence of meso-DAP in cell wall, ascribe this strain to the genus Actinoplanes. The pigmentation and morphological characteristics together with the cultural and physiological features distinguish this strain from all the described Actinoplanes species. It is considered to be a new species for which the name Actinoplanes deccanensis nov. sp. is proposed. Lipiarmycin is produced in an organic complex medium containg NaCl. Production occurs at the end of trophophase and continues, though at decreasing rate, during idiophase.

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Lipiarmycin, a metabolite of Actinoplanes deccanensis nov. sp. (PARENTI et al.), has been isolated in pure form. It has a molecular formula C₅₂-54H₇₄-76Cl₂O₁₉, (M.W.=1, 073-1, 099). From its chemical and physico-chemical characteristics, lipiarmycin can be considered a new antibiotic. Lipiarmycin is highly active against Gram-positive bacteria, including strains resistant to the medically important antibiotics and protects mice experimentally infected with Streptococcus haemolyticus. Lipiarmycin inhibits growth of susceptible bacteria by interfering with RNA synthesis.

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A new water-soluble basic antibiotic named antibiotic A-16316-C was isolated together with antibiotic A-396-I and hygromycin B from a streptomyces strain identified as Streptoverticillium eurocidicus. The properties of the antibiotic A-16316-C were similar to those of destomycin B. But, it was found that the antibiotic A-16316-C was not identical with destomycin B on the basis of NMR analysis. On acidic degradation antibiotic A-16316-C gave N, N'-dimethyl-2-deoxystreptamine, destomic acid and D-mannose. The gross structure for antibiotic A-16316-C was deduced from chemical reactions and spectral data.

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Derinamycin was isolated from the mycelium of Streptomyces venezuelae Tü 1102 and its molecular formula was tentatively assigned as C₅₁H₉₃NO₂₃. The antibiotic inhibits the growth of fungi, gram-positive bacteria and certain gram-negative bacteria but is less active against yeasts. A study of derinamycin action on the macromolecular synthesis of intact Bacillus subtilis revealed that the antibiotic suppressed DNA and RNA syntheses but that protein synthesis was less affected. Derinamycin exerted no selective inhibition between DNA and RNA syntheses in the double-isotope experiment used to assess the relative effects of the antibiotic.

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Streptovirudin is a complex of antibiotics isolated from fermentation of a Streptomyces strain. Eight components have been isolated as pure substances, designated as streptovirudins A₁, A₂, B₁, B₂, C₁, C₂, D₁ and D₂. The streptovirudins are chemically and biologically related to each other and appear to be a new family of antibiotics exhibiting activity against a variety of Gram-positive bacteria, mycobacteria, and various DNA- and RNA-viruses. According to their physico-chemical properties these antibiotics have been classified in series I and II. The streptovirudins of series II (A₂, B₂, C₂, D₂) are related to the reported antibiotics tunicamycin, mycospocidin and 24010.

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SS-228Y, an antibiotic produced by Chainia sp., has been established as a benz(a)-anthraquinone derivative by spectroscopic evidence.

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The structure of the antibiotic althiomycin has been determined by a combination of chemical and physical methods.

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Tuberactinamine N, the cyclic peptide moiety of tuberactinomycin N, was obtained in a crystalline state through liberation of γ-hydroxy-β-lysine from tuberactinomycin N by acid treatment. Tuberactinamine N possesses an intramolecular hydrogen bond in its molecule and showed antibacterial activities comparable to those of the original antibiotics. Conversion of tuberactinomycin N to O was achieved through coupling of diacyl-β-lysine with tuberactinamine N followed by removal of the protecting groups.

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α- or β-Glucosidic linkage of validamycin was selectively cleaved by microbial hydrolysis, and especially the conversion of validamycin C into validamycin A by the selective hydrolysis of α-glucosidic linkage has important significance because validamycin C is considerably less active than validamycin A. Semisyntheses of validamycins including a new validamycin, β-D-galactosyl-validoxylamine A were carried out by microbial transglycosidation using validoxylamine A as a glycosyl acceptor. D-[U-¹⁴C]glucose and [¹⁴C]validoxylamine A were highly incorporated into validamycin A by validamycin-producing Streptomyces hygroscopicus var.limoneus.

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Growing cultures, as well as broken and lyophilized cells of pseudomonas 56 were found to degrade erythromycin A, and lyophilized cells inactivated erythromycins A and B. The enzyme system involved in this degradation was constitutive and the enzyme level in the cells could be increased about 8-fold when oleandomycin or erythromycin B was added to the growth medium. The ability of whole or broken cells to inactivate erythromycin A was completely lost when these preparations were boiled, and the erythromycin A-inactivating activity was localized in the cell membrane fraction. The lyophilized cells did not degrade oleandomycin, methymycin, tylosin, a mixture of leucomycins, josamycin, or maridomycin III.

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A homologue series of aliphatic streptomycylamines (SM-amines) have been prepared and tested in vitro (binding to 70S ribosomes) and in vivo (MIC). The short-chain SM-amines act as streptomycin (SM) but are less active than SM. They are inactive towards a SM-resistant Escherichia coli, our strain 042. The long-chain SM-amines are active both towards our sensitive and resistant E. coli, our strains 079 and 042. Their activities are not pH-dependent in contrast to that of SM. However, the higher homologues of the aliphatic amines (C₁₀-C₁₆) are considerably active per se although two to four times less than the corresponding SM-amines. Further, the amines do not compete with the SM-amine for the binding to the ribosomal particles. The binding affinities of these long-chain SM-amines to ribosomes are considerably smaller than that of SM. The binding is however specific as a typical isotope dilution curve can be obtained. We conclude that the long-chain SM-amines have a mode of action different from that of SM.

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Distribution and balance studies with carbon-14-labeled amphotericin B methyl ester (AME) were carried out in mice. The radioactive AME was administered by either the intraperitoneal (i.p.) or intravenous (i.v.) route. In the organ distribution study, the percent radioactivity accumulating in the lung of i.v. treated mice at 1 hour after administration was about 150 times greater than that observed when the intraperitoneal route was used. No accumulation of radioactivity with time was detected in the kidneys of either the i.v. or i.p. treated mice. After 4 days, about 51% of the total radioactivity was excreted into the urine and feces of mice after i.v. administration, but only about 15% of the total radioactivity was excreted in the case of mice receiving radioactive AME by the i.p. route. In the identification of the substances excreted in the urine, thin-layer chromatography (TLC), radioactivity, and bioautographic evidence suggest that there was no detectable de-esterification of AME to the parent compound in mice treated either intraperitoneally or intravenously with AME.

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Oxamicetin was tested against 12 strains of parasitic leptospira each representing a different serotype and serogroup, and 8 saprophytic strains in liquid media. The results showed general susceptibility of parasitic leptospira being MIC's from 0.1 to 0.5μg/ml. The MIC's against saprophytic strains were 10-40μg/ml.

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