Ontology highlight
ABSTRACT:
SUBMITTER: Godbout R
PROVIDER: S-EPMC5106009 | biostudies-literature | 2016
REPOSITORIES: biostudies-literature
Godbout Raphaël R Légaré Sébastien S Auger Maud M Carpentier Claudia C Otis François F Auger Michèle M Lagüe Patrick P Voyer Normand N
PloS one 20161111 11
A novel 21-residue peptide incorporating six fluorinated amino acids was prepared. It was designed to fold into an amphiphilic alpha helical structure of nanoscale length with one hydrophobic face and one fluorinated face. The formation of a fluorous interface serves as the main vector for the formation of a superstructure in a bilayer membrane. Fluorescence assays showed this ion channel's ability to facilitate the translocation of alkali metal ions through a phospholipid membrane, with selecti ...[more]