Translocation of an Aib-containing peptide through cell membranes.
The biophysical characteristics and channel-forming activity of peptaibols inserted into artificial membranes have been studied over the last 30 years. However, to our knowledge, no studies have addressed directly their behavior in living cells. In this work, a novel strategy has been employed to precisely assess the living cell membrane-penetrating activity of a fluorescein-labeled Aib (alpha-aminoisobutyric acid)-containing peptide derived from a peptaibol, trichorovin-XIIa (TV-XIIa). We have demonstrated for the first time that the peptide containing an unusual amino acid residue, Aib, is taken up by cells via a non endocytic pathway. The replacement of Aib in the TV-XIIa sequence with Ala inhibits the cellular uptake.
Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan. wada@gly.oups.ac.jp
Shun-ichi
S
Wada
Yasunari
Y
Hitora
Reiko
R
Tanaka
Hidehito
H
Urata
D000621:Aminoisobutyric Acids / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D001703:Biophysics / Q000379:methods; D045744:Cell Line, Tumor; D002462:Cell Membrane / Q000187:drug effects* / Q000378:metabolism; D002469:Cell Separation; D002626:Chemistry, Pharmaceutical / Q000379:methods; D015195:Drug Design; D005434:Flow Cytometry; D019793:Fluorescein / Q000737:chemistry; D006801:Humans; D051379:Mice; D018613:Microscopy, Confocal; D041681:NIH 3T3 Cells; D054848:Peptaibols / Q000737:chemistry* / Q000378:metabolism; D010455:Peptides / Q000737:chemistry
D000621:Aminoisobutyric Acids; D054848:Peptaibols; D010455:Peptides; C532914:trichorovin-XIIa; C100049:2-aminoisobutyric acid; D019793:Fluorescein