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PDBsum entry 1d9m
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Membrane protein
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PDB id
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1d9m
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References listed in PDB file
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Key reference
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Title
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Nmr structural characterization of cecropin a(1-8) - Magainin 2(1-12) and cecropin a (1-8) - Melittin (1-12) hybrid peptides.
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Authors
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D.Oh,
S.Y.Shin,
J.H.Kang,
K.S.Hahm,
K.L.Kim,
Y.Kim.
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Ref.
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J Pept Res, 1999,
53,
578-589.
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PubMed id
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Abstract
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In order to elucidate the structure-antibiotic activity relationships of the
peptides, the three-dimensional structures of two hybrid peptides, CA(1-8) -
MA(1-12) and CA(1-8) - ME(1-12) in trifluoroethanol-containing aqueous solution
were investigated by NMR spectroscopy. Both CA(1-8) - MA(1-12) and CA(1-8) -
ME(1-12) have strong antibacterial activity but only CA(1-8) - ME(1-12) has
hemolytic activity against human erythrocytes. CA(1-8) - MA(1-12) has a
hydrophobic 310-helix of only two turns combined with one short helix in the
N-terminus with a flexible hinge section in between. CA(1-8) - MA(1-12) has a
severely bent structure in the middle of the peptide. These structural features
as well as the low hydrophobicity of CA(1-8) - MA(1-12) seem to be crucial for
the selective lysis against the membrane of prokaryotic cells. CA(1-8) -
ME(1-12) has an alpha-helical structure of about three turns in the melittin
domain and a flexible structure with one turn in the cecropin domain connected
with a flexible hinge section in between, and these might be the structural
features required for membrane disruption against prokaryotic and eukaryotic
cells. The central hinge region (Gly9-Ile10-Gly11) in an amphipathic
antibacterial peptide is considered to play an important role in providing the
conformational flexibility required for ion channel formation of the C-terminal
hydrophobic alpha-helix on cell membrane.
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