| Autor: |
Teta R; The NeaNat Group, Dipartimento di Farmacia, Università degli Studi di Napoli Federico II , Via D. Montesano 49, 80131 Napoli, Italy., Marteinsson VT; Matis ohf. , Vinlandsleid 12, 113 Reykjavik, Iceland.; Faculty of Food Science and Nutrition, University of Iceland , Saemundargata 2, 101 Reykjavik, Iceland., Longeon A; Laboratoire Molécules de Communication et Adaptation des Micro-organismes, UMR 7245 CNRS, Muséum National d'Histoire Naturelle , 57 Rue Cuvier (C.P. 54), 75005 Paris, France., Klonowski AM; Matis ohf. , Vinlandsleid 12, 113 Reykjavik, Iceland., Groben R; Matis ohf. , Vinlandsleid 12, 113 Reykjavik, Iceland., Bourguet-Kondracki ML; Laboratoire Molécules de Communication et Adaptation des Micro-organismes, UMR 7245 CNRS, Muséum National d'Histoire Naturelle , 57 Rue Cuvier (C.P. 54), 75005 Paris, France., Costantino V; The NeaNat Group, Dipartimento di Farmacia, Università degli Studi di Napoli Federico II , Via D. Montesano 49, 80131 Napoli, Italy., Mangoni A; The NeaNat Group, Dipartimento di Farmacia, Università degli Studi di Napoli Federico II , Via D. Montesano 49, 80131 Napoli, Italy. |
| Abstrakt: |
The thermophilic bacterium Thermoactinomyces vulgaris strain ISCAR 2354, isolated from a coastal hydrothermal vent in Iceland, was shown to contain thermoactinoamide A (1), a new cyclic hexapeptide composed of mixed d and l amino acids, along with five minor analogues (2-6). The structure of 1 was determined by one- and two-dimensional NMR spectroscopy, high-resolution tandem mass spectrometry, and advanced Marfey's analysis of 1 and of the products of its partial hydrolysis. Thermoactinoamide A inhibited the growth of Staphylococcus aureus ATCC 6538 with an MIC value of 35 μM. On the basis of literature data and this work, cyclic hexapeptides with mixed d/l configurations, one aromatic amino acid residue, and a prevalence of lipophilic residues can be seen as a starting point to define a new, easily accessible scaffold in the search for new antibiotic agents. |
