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NMR solution structure and position of transportan in neutral phospholipid bicelles.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. biofysik. (Astrid Gräslund)
2004 (English)In: FEBS Lett, ISSN 0014-5793, Vol. 567, no 2-3, 265-9 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2004. Vol. 567, no 2-3, 265-9 p.
Keyword [en]
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
URN: urn:nbn:se:su:diva-22322PubMedID: 15178334OAI: diva2:188849
Available from: 2007-06-12 Created: 2007-06-12 Last updated: 2011-01-12Bibliographically approved

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Bárány-Wallje, ElsaGräslund, AstridMäler, Lena
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