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NMR solution structure and position of transportan in neutral phospholipid bicelles.

Bárány-Wallje, Elsa (author)
Stockholms universitet,Institutionen för biokemi och biofysik,biofysik,Astrid Gräslund
Andersson, August (author)
Gräslund, Astrid (author)
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Mäler, Lena (author)
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 (creator_code:org_t)
2004
2004
English.
In: FEBS Lett. - 0014-5793. ; 567:2-3, s. 265-9
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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 -helix in the C-terminal mastoparan part of the peptide and a weaker tendency to form an -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.

Keyword

Amides/chemistry
Amino Acid Sequence
Circular Dichroism
Dimyristoylphosphatidylcholine/*chemistry
Drug Carriers/chemistry
Galanin
Glycerophosphates/chemistry
Lipid Bilayers/*chemistry
Micelles
Models; Molecular
Molecular Sequence Data
Nuclear Magnetic Resonance; Biomolecular/*methods
Phospholipid Ethers/*chemistry
Phosphorylcholine/*analogs & derivatives/chemistry
Protein Structure; Secondary
Protein Structure; Tertiary
Recombinant Fusion Proteins/*chemistry
Spin Labels
Wasp Venoms

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