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The NK‐lysin derived peptide NK‐2 preferentially kills cancer cells with increased surface levels of negatively charged phosphatidylserine
Author(s) -
Schröder-Borm Hannah,
Bakalova Rumiana,
Andrä Jörg
Publication year - 2005
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/j.febslet.2005.09.084
Subject(s) - phosphatidylserine , lysin , liposome , peptide , cancer cell , chemistry , cell culture , cell , förster resonance energy transfer , cytotoxicity , biophysics , microbiology and biotechnology , biochemistry , fluorescence , biology , membrane , cancer , in vitro , gene , phospholipid , escherichia coli , genetics , physics , quantum mechanics , bacteriophage
The NK‐lysin derived peptide NK‐2 is a potent antibacterial, but non‐toxic to a human keratinocyte cell line and of low hemolytic activity. Its target selectivity is based upon a strong binding preference to membranes containing anionic phospholipids, which are normally not found on the surface of human cells. Here, we analyzed the interaction of NK‐2 with normal human lymphocytes and seven different human cancer cell lines and demonstrate that some of these cells expose negatively charged surface phosphatidylserine (PS), which presumably facilitates killing of the cells by NK‐2. This is underlined by the specific intercalation of the peptide into PS‐containing liposomes analyzed by fluorescence‐resonance energy transfer spectroscopy.