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Parallel and antiparallel dimers of magainin 2: their interaction with phospholipid membrane and antibacterial activity
Author(s) -
Mukai Yasuhiro,
Matsushita Yuko,
Niidome Takuro,
Hatekeyama Tomomitsu,
Aoyagi Haruhiko
Publication year - 2002
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.416
Subject(s) - antiparallel (mathematics) , chemistry , membrane , magainin , liposome , monomer , phospholipid , biophysics , phosphatidylcholine , vesicle , lipid bilayer , antibacterial activity , quenching (fluorescence) , peptide , fluorescence , stereochemistry , biochemistry , antimicrobial peptides , organic chemistry , bacteria , biology , physics , genetics , quantum mechanics , magnetic field , polymer
Magainin 2 (M2) forms pores by associating with several other M2 molecules in lipid membranes and shows antibacterial activity. To examine the effect of M2 dimerization on biological activity and membrane interaction, parallel and antiparallel M2 dimers were prepared from two monomeric precursors. Antibacterial and haemolytic activities were enhanced by dimerization. CD measurements showed that both dimers and monomers have an α‐helical structure in the presence of lipid vesicles. Tryptophan fluorescence shift and KI quenching studies showed that all the peptides were more deeply embedded in acidic liposomes than in neutral liposomes. Experiments on dye‐leakage activity and membrane translocation of peptides suggest that dimers and monomers form pores through lipid membranes, although the pore formation may be accompanied by membrane disturbance. Although dimerization of M2 increased the interaction activity with lipid membranes, no appreciable difference between the activities of parallel and antiparallel M2 dimers was observed. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.