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The position of the cell penetrating peptide penetratin in SDS micelles determined by NMR
Author(s) -
Lindberg Mattias,
Gräslund Astrid
Publication year - 2001
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/s0014-5793(01)02433-4
Subject(s) - micelle , chemistry , peptide , antennapedia , cell penetrating peptide , amide , helix (gastropod) , solvent , biophysics , biochemistry , transcription factor , organic chemistry , aqueous solution , homeobox , biology , gene , ecology , snail
Penetratin is a 16 residue peptide, RQI KIWFQ NRRMK WKK‐amide, with the ability to penetrate cell membranes and a sequence taken from the homeodomain of the Drosophila Antennapedia transcription factor. 600 MHz 1 H‐nuclear magnetic resonance has been used to study the structure and location of penetratin interacting with a sodium dodecyl sulphate micelle. The positioning of penetratin in the micelle was studied by adding paramagnetic probes (Mn 2+ ions, 5‐doxyl and 12‐doxyl stearic acid) to the solvent. The results show that the peptide is a straight helix positioned with its C‐terminus deep inside the micelle and its N‐terminus near the surface of the micelle.