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Differences in membrane pore formation by peptaibols
Author(s) -
Grigoriev Pavel A.,
Schlegel Brigitte,
Kronen Matthias,
Berg Albrecht,
Härtl Albert,
Gräfe Udo
Publication year - 2003
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.502
Subject(s) - alamethicin , chemistry , membrane , amino acid , peptide , biophysics , biochemistry , bilayer , biology
The efficiencies of membrane pore formation by 14 naturally occurring peptaibols and two structurally modified ampullosporins were compared using an artificial bilayer membrane model. Major differences were found in the dependence on peptide sequences and the constituting amino acids. Alamethicin F‐30, chrysospermins C/D, paracelsin and texenomycin A displayed higher activity by several orders of magnitude in comparison with smaller peptaibols containing <17 amino acids such as ampullosporins, trichofumins, bergofungins and cephaibols. Biological activities such as the induction of pigment formation by the fungus Phoma destructiva and long acting hypothermia and depression of locomotor activity in mice were correlated with moderate membrane permeabilization. No or weak membrane activities corresponded with biological inactivity. Highly membrane‐active structures such as alamethicin F‐30, chrysospermin C, texenomycin A and paracelsin A displayed antibiotic effects against the fungus and toxicity in mice. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.