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Lipid membrane binding of NK‐lysin
Author(s) -
Ruysschaert Jean-Marie,
Goormaghtigh Erik,
Homblé F,
Andersson Mats,
Liepinsh Edvards,
Otting Gottfried
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00261-0
Subject(s) - lysin , chemistry , biophysics , biochemistry , biology , escherichia coli , gene , bacteriophage
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 Trp 58 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 non‐specific 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 α‐helices as the predominant conformation. The molecular mechanism of the membrane‐destabilizing effect of NK‐lysin is discussed.