Reverse phase liquid chromatography of beta-endorphins and related peptides.

Anomalous band broadening of beta-endorphin related polypeptides chromatographed on hydrophobic high performance stationary phases can be attributed to ligand induced conformational changes associated with polypeptide folding. In the presence of anionic lipids the size exclusion chromatographic behaviour of members of the beta-endorphin family also exhibits similar behaviour. These structure-retention and band broadening behaviour of these polypeptides were in accord with predictions made by hydropathy algorithms and amphipathic helix representations. These observations on surface accessibility of key amino acid residues and their interaction as a conformationally induced domains with stationary phase ligands are equally relevant to other peptidic solutes and neurotransmitters.