Premium
Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment
Author(s) -
Wieprecht Torsten,
Dathe Margitta,
Krause Eberhard,
Beyermann Michael,
Maloy W.Lee,
MacDonald Dorothy L,
Bienert Michael
Publication year - 1997
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(97)01266-0
Subject(s) - circular dichroism , magainin , chemistry , amphiphile , vesicle , antibacterial activity , hydrophobic effect , membrane , biophysics , peptide , phospholipid , biochemistry , stereochemistry , antimicrobial peptides , organic chemistry , bacteria , biology , copolymer , genetics , polymer
Starting from the sequences of magainin 2 analogs, peptides with slightly increased hydrophobic moment ( μ ) but retained other structural parameters were designed. Circular dichroism investigations revealed that all peptides adopt an α‐helical conformation when bound to phospholipid vesicles. Analogs with increased μ were considerably more active in permeabilizing vesicles mainly composed of zwitterionic lipid. In addition, the antibacterial and hemolytic activities of these analogs were enhanced. Correlation of permeabilization and binding indicated that the activity increase is predominantly caused by an increased membrane affinity of the peptides due to strengthened hydrophobic interactions.