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Yamnitz CR, Gokel GW: Synthetic, biologically active amphiphilic peptides. Chem Biodivers. 2007 Jun;4(6):1395-412.
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. |
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