The purification of peptides by partition chromatography based on a hydrophobicity scale.
A study of the efficiency of partition chromatography for the purification of peptides as a function of structure has been undertaken. A series of 19 omission analogs of camel beta-endorphin and of some of its partial sequences have been synthesized with each analog missing only a single amino acid. Their chromatographic properties have been examined with use of the Martin hypothesis and the RM concept, and a hydrophobicity scale for the amino acid side chains was obtained. To a first approximation a correlation with the Tanford hydrophobicity scale for amino acids was found. A decrease in hydrophobicity has been observed with increasing chain length and is discussed in terms of column efficiencies required for the purification of synthetic peptides.
D000595:Amino Acid Sequence; D002845:Chromatography / Q000379:methods*; D004723:Endorphins / Q000138:chemical synthesis; D008956:Models, Chemical; D010455:Peptides / Q000302:isolation & purification*
D004723:Endorphins; D010455:Peptides