Thermoactinoamide A, an Antibiotic Lipophilic Cyclopeptide from the Icelandic Thermophilic Bacterium Thermoactinomyces vulgaris

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 d...

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Bibliographic Details
Published in:Journal of Natural Products
Main Authors: TETA, ROBERTA, Marteinsson, Viggó Thór, Longeon, Arlette, Klonowski, Alexandra M, Groben, René, Bourguet Kondracki, Marie Lise, COSTANTINO, VALERIA, MANGONI, ALFONSO
Other Authors: Teta, Roberta, Costantino, Valeria, Mangoni, Alfonso
Format: Article in Journal/Newspaper
Language:English
Published: 2017
Subjects:
cyclic peptide
thermophilic bacteria
structure elucidation
absolute configuration
antibacterial activity
Iceland
Online Access:http://hdl.handle.net/11588/683648
https://doi.org/10.1021/acs.jnatprod.7b00560
Description
Summary: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.

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