Synthetic, Biologically Active Amphiphilic Peptides

Amphiphilic peptides typically consist of a peptide portion that may be 5–25 (or more) amino acids in length. The hydrophobic portion may be a single fatty acid residue, but can also be more elaborate. The main focus of this article lies on the family of synthetic anion binders (SATs) of the general structure (R 1 ) 2 N‐COCH 2 OCH 2 CO‐(Aaa) n ‐OR 3 . The most‐common R 1 group is the octadecyl (C 18 H 37 ) group. The most studied peptide sequence in this family is (Gly) 3 ‐Pro‐(Gly) 3 , although different sequences (and longer and shorter peptides) have been prepared as well. The C‐terminal ester residue providing the most effective anion release from liposomes is heptyl (C 7 H 15 ), although many others have been examined. The compound (C 18 H 37 ) 2 N‐COCH 2 OCH 2 CO‐(Gly) 3 ‐Pro‐(Gly) 3 ‐OBn (Bn=benzyl) was found to mediate Cl − transport in mouse epithelial cells.