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.
Kassim
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SY
Department of Chemistry and Biochemistry, University of Maryland, Baltimore County 21250, USA.
Restrepo
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Kalivretenos
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D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D017630:Connexins / Q000737:chemistry; D007473:Ion Channels / Q000378:metabolism*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000302:isolation & purification; D010455:Peptides / Q000138:chemical synthesis* / Q000302:isolation & purification; D017433:Protein Structure, Secondary; D051381:Rats; D013056:Spectrophotometry, Ultraviolet
D017630:Connexins; D007473:Ion Channels; D009842:Oligopeptides; D010455:Peptides