Abstract
Transportan is a chimeric cell-penetrating peptide constructed from the peptides galanin and mastoparan, which has the ability to internalize living cells carrying a hydrophilic load. In this study, we have determined the NMR solution structure and investigated the position of transportan in neutral bicelles. The structure revealed a well-defined alpha-helix in the C-terminal mastoparan part of the peptide and a weaker tendency to form an alpha-helix in the N-terminal domain. The position of the peptide in relation to the membrane, as studied by adding paramagnetic probes, shows that the peptide lies parallel to, and in the head-group region of the membrane surface. This result is supported by amide proton secondary chemical shifts.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amides / chemistry
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Amino Acid Sequence
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Circular Dichroism
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Dimyristoylphosphatidylcholine / chemistry*
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Drug Carriers / chemistry
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Galanin
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Glycerophosphates / chemistry
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Lipid Bilayers / chemistry*
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Micelles
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular / methods*
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Phospholipid Ethers / chemistry*
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Phosphorylcholine / analogs & derivatives*
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Phosphorylcholine / chemistry
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / chemistry*
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Spin Labels
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Wasp Venoms
Substances
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1,2-dihexadecyl-sn-glycero-3-phosphocholine
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Amides
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Drug Carriers
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Glycerophosphates
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Lipid Bilayers
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Micelles
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Phospholipid Ethers
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Recombinant Fusion Proteins
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Spin Labels
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Wasp Venoms
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transportan
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Phosphorylcholine
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dodecylphosphocholine
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Galanin
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Dimyristoylphosphatidylcholine