par Ruysschaert, Jean Marie 
;Goormaghtigh, Erik ;Homblé, Fabrice ;Andersson, M;Liepinsh, E;Otting, G
Référence FEBS letters, 425, 2, page (341-344)
Publication Publié, 1998-03
;Goormaghtigh, Erik ;Homblé, Fabrice ;Andersson, M;Liepinsh, E;Otting, GRéférence FEBS letters, 425, 2, page (341-344)
Publication Publié, 1998-03
Article révisé par les pairs
| Résumé : | The membrane-binding properties and pore-forming potential of the tumor-lysing and antibacterial polypeptide NK-lysin were investigated. Fluorescence quenching experiments show a drastic change of accessibility to Trp58 in solution and in association with a lipid membrane. Calcein release from large unilamellar vesicles and fluctuating conductivity observed across a planar lipid bilayer of asolectin show that NK-lysin renders lipid bilayers permeable in a transient fashion, indicating a nonspecific lipid interaction as the mechanism underlying the biological activity. FTIR experiments show the same amount and type of regular secondary structure of NK-lysin in the membrane as in aqueous solution and exclude a structural rearrangement into a set of parallel or antiparallel alpha-helices as the predominant conformation. The molecular mechanism of the membrane-destabilizing effect of NK-lysin is discussed. |
