Structural highlights
Publication Abstract from PubMed
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.
NMR solution structure and position of transportan in neutral phospholipid bicelles.,Barany-Wallje E, Andersson A, Graslund A, Maler L FEBS Lett. 2004 Jun 4;567(2-3):265-9. PMID:15178334[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Barany-Wallje E, Andersson A, Graslund A, Maler L. NMR solution structure and position of transportan in neutral phospholipid bicelles. FEBS Lett. 2004 Jun 4;567(2-3):265-9. PMID:15178334 doi:http://dx.doi.org/10.1016/j.febslet.2004.04.079
