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Updated: Jul 4, 2026

Measuring Peptide Translocation into Large Unilamellar Vesicles
Published on: January 27, 2012
Translocation of an Aib-containing peptide through cell membranes
Shun-ichi Wada1, Yasunari Hitora, Reiko Tanaka
1Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan. wada@gly.oups.ac.jp
Abstract:
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.
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