Lipid membrane binding of NK-lysin

FEBS Lett. 1998 Mar 27;425(2):341-4. doi: 10.1016/s0014-5793(98)00261-0.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Infective Agents / metabolism*
  • Lipid Bilayers / metabolism*
  • Models, Molecular
  • Proteolipids / metabolism*
  • Pulmonary Surfactants / metabolism*


  • Anti-Infective Agents
  • Lipid Bilayers
  • NK-lysin
  • Proteolipids
  • Pulmonary Surfactants