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Membrane Permeabilisation and Antimycoplasmic Activity of the 18-residue Peptaibols, Trichorzins PA

L Béven, D Duval, S Rebuffat, F G Riddell, B Bodo, H Wróblewski

Biochim Biophys Acta. 1998 Jun 24;1372(1):78-90.

PMID: 9651487

Abstract:

The membrane permeabilisation properties of six linear natural 18-residue peptaibols, termed trichorzins PA, have been assessed on liposomes and on mollicutes (trivial name, mycoplasmas), a class of parasitic bacteria characterized by a small genome, the lack of a cell wall, a minute cell size, and the incorporation in their plasma membrane of exogenously supplied cholesterol. The trichorzins PA used in this study (PA II, PA IV-VI, PA VIII, and PA IX) differ between them by amino acid or amino alcohol substitutions at positions 4, 7, and 18, and form slightly amphipathic alpha-helices. They proved bactericidal for mollicutes belonging to the genera Acholeplasma, Mycoplasma, and Spiroplasma, with minimal inhibitory concentrations (3.12

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AP174752422 Sodium ionophore VIII Sodium ionophore VIII 174752-42-2 Price
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