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

• 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.

Nyckelord

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

Publikations- och innehållstyp

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