Synthesis and purification of hydrophobic peptides for use in biomimetic ion channels

The synthesis and subsequent purification of several hydrophobic peptides is described. These peptides include the 24-residue M3 transmembrane domain of the rat connexin 32 protein, a peptide sequence that contains only seven amino acids with hydrophilic side-chains (71% hydrophobic). Moreover, for comparison, a much smaller hydrophobic octapeptide, designed to exist with alpha-helical secondary structure, was also studied. Optimum conditions for the RP-HPLC purification of these peptides was dependent on peptide length and solubility properties.