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NMR solution structure and position of transportan in neutral phospholipid bicelles
Author(s) -
Bárány-Wallje Elsa,
Andersson August,
Gräslund Astrid,
Mäler Lena
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.04.079
Subject(s) - mastoparan , peptide , chemistry , helix (gastropod) , amide , membrane , amphiphile , model lipid bilayer , phospholipid , biophysics , stereochemistry , lipid bilayer , biochemistry , copolymer , organic chemistry , biology , ecology , receptor , g protein , lipid bilayer phase behavior , snail , polymer
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 α‐helix in the C‐terminal mastoparan part of the peptide and a weaker tendency to form an α‐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.