Synthetic, Biologically Active Amphiphilic Peptides

Abstract

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 groups are octadecyl (C 18 H 37 ). 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.

Docetaxel Nanotechnology in Anticancer Therapy

“…It is difficult to deduce a mechanism for the destabilizing activity of DM‐DAP 2+ on the basis of our data. Several papers have been published35, 36 on the capacity of monomolecules (ligand‐assembled π slides,37, 38 membrane‐active rigid‐rod molecules,39 bioinspired peptide,40, 41 calix[4]arene derivatives),42 self‐assembled molecules,43 or mobile carriers44 to orient transmembrane and form stable pores in the phospholipidic bilayer for passive ion or active electron transport, but DM‐DAP 2+ cannot cross right through the bilayer and the formation of a stable channel in the present case is not feasible. We hypothesize that this species could favor the formation of transient pores in the membrane owing to its affinity for the liposomal bilayer (see Section 2.2) combined with a considerable hydrophilic character.…”

The water-channel forming ability of heptapeptide-based anion channels: insights from molecular dynamics simulations

“…A number of reviews on synthetic ion transporters along with a discussion of pertinent design criteria have been published. [10][11][12][13][14][15][16][32][33][34][35][36] Similar to the SCMTR class of compounds, cyclic peptide nanotubes rely on the amino acids as the primary building block, and function through a stacking mechanism. [37][38][39][40][41][42][43][44] Acyclic compounds like isophthalamides 45,46 and dianilides 47 are also thought to stack in order to function as a channel.…”

Amino acid containing anion receptors

“…In subsequent work the structure of 1a was systematically varied to evaluate the influence of each subunit on anion transport. These investigations, that have been reviewed 33 revealed that the structures of the N-terminal and the C-terminal anchor chains, the structure of the midpolar regime, as well as the length and sequence of the peptide chain in 1a have profound effects on the rate with which chloride release from liposomes can be achieved. Replacement of the proline residue by leucine or pipecolinic acid, for example, the latter of which is nearly identical in size, shape, and polarity as proline, caused a significant loss of activity.…”