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Effects of peptide dimerization on pore formation: Antiparallel disulfide‐dimerized magainin 2 analogue
Author(s) -
Hara Toshiaki,
Kodama Hiroaki,
Kondo Michio,
Wakamatsu Kaori,
Takeda Akemi,
Tachi Tomoya,
Matsuzaki Katsumi
Publication year - 2001
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(20010405)58:4<437::aid-bip1019>3.0.co;2-i
Subject(s) - chemistry , dimer , antiparallel (mathematics) , monomer , magainin , peptide , crystallography , lipid bilayer , supramolecular chemistry , covalent bond , membrane , stereochemistry , biophysics , biochemistry , organic chemistry , antimicrobial peptides , crystal structure , physics , quantum mechanics , magnetic field , biology , polymer
To elucidate the effects of peptide dimerization on pore formation by magainin 2 (MG2), a covalently linked antiparallel dimer of the MG2 analogue [(F5Y, L6C, F16W, I20C‐MG2) 2 : II ] was synthesized based on the dimer structure revealed by our NMR study. The interactions of the dimer with lipid bilayers were investigated by CD and fluorescence in comparison with a monomer analogue (F5Y, F16W‐MG2: I ). Similar to I , II was found to form a peptide–lipid supramolecular complex pore accompanied with lipid flip‐flop and peptide translocation. The pore formed by II was characterized by a slightly larger pore diameter and a threefold longer lifetime than that of I , although the pore formation rate of the dimer was lower than that of the monomer. The coexistence of the dimer and the monomer exhibited slight but significant synergism in membrane permeabilization, which was maximal at a monomer/dimer ratio of 3. Therefore, we concluded that a pentameric pore composed of one pore‐stabilizing dimer and three monomers maximized the overall leakage activity in keeping with our kinetic prediction. © 2001 John Wiley & Sons, Inc. Biopolymers 58: 437–446, 2001