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PDBsum entry 1dum
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Antimicrobial protein
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PDB id
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1dum
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References listed in PDB file
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Key reference
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Title
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Effects of peptide dimerization on pore formation: antiparallel disulfide-Dimerized magainin 2 analogue.
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Authors
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T.Hara,
H.Kodama,
M.Kondo,
K.Wakamatsu,
A.Takeda,
T.Tachi,
K.Matsuzaki.
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Ref.
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Biopolymers, 2001,
58,
437-446.
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PubMed id
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Abstract
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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.
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