Structural elucidation of trikoningins KA and KB, peptaibols from Trichoderma koningii

Autor:	Catherine Auvin-Guette, Marcel Massias, Isabelle Vuidepot, Bernard Bodo, Sylvie Rebuffat
Rok vydání:	1993
Předmět:	chemistry.chemical_classification Trichoderma koningii biology Stereochemistry Peptaibol Biological activity Peptide Fungi imperfecti biology.organism_classification medicine.disease_cause chemistry.chemical_compound chemistry Staphylococcus aureus medicine
Zdroj:	Journal of the Chemical Society, Perkin Transactions 1. :249
ISSN:	1364-5463 0300-922X
DOI:	10.1039/p19930000249
Popis:	A Trichoderma koningii strain collected in Uruguay produced two antibiotic membrane-active peptidic groups, the trikoningins KA and KB, from which the main components KA V, KB I and KB II were purified. The peptide sequences were elucidated by FAB mass spectrometry and high-field NMR experiments. KA V was a nonadecapeptaibol, whereas KB I and KB II were two 11-residue lipopeptaibols. They all displayed antibiotic activity against Staphylococcus aureus. Their membrane-modifying properties were examined by following the leakage of liposome-entrapped carboxyfluorescein. KA V induced similar permeability modifications to those exhibited by known 19-residue peptaibols, while the KB I and KB II activities were weaker.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::01d22e2566c5833fd098600e315948b4 https://doi.org/10.1039/p19930000249 Zobrazit plný text záznamu