Synthetic, Biologically Active Amphiphilic Peptides

✍ Scribed by Carl R. Yamnitz; George W. Gokel

• Publisher: John Wiley and Sons
• Year: 2007
• Tongue: English
• Weight: 310 KB
• Volume: 4
• Category: Article
• ISSN: 1612-1872
• DOI: 10.1002/cbdv.200790119

✦ Synopsis

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 ¼ benzyl) was found to mediate Cl À transport in mouse epithelial cells.