title: Physicochemical studies of biologically active peptides by low-temperature reversed-phase high-performance liquid chromatography.
abstract: The high-performance liquid chromatographic separation of biologically active peptides containing 1-prolyl residues is demonstrated. Rapid isomer interconversion between cis- and trans-isomeric forms at the prolyl peptide bond is shown to produce classical secondary equilibrium effects in the peak shapes. By operating the column at temperatures in the range -15 degrees C to 5 degrees C it is possible to obtain normal separations of the various isomeric forms. The use of low column temperatures makes physicochemical studies possible, e.g., the effect of pH on isomer composition in free solution as reported here for morphiceptin.
authors.affiliation: Department of Chemistry, Trinity College, Hartford, CT 06106.
authors.forename: D E
authors.initials: DE
authors.lastname: Henderson
authors.forename: J A
authors.initials: JA
authors.lastname: Mello
mesh_terms: D000700:Analgesics / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D004723:Endorphins / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D010455:Peptides / Q000032:analysis* / Q000502:physiology; D011392:Proline / Q000032:analysis; D013696:Temperature
chemical_list: D000700:Analgesics; D004723:Endorphins; D010455:Peptides; C028889:morphiceptin; D011392:Proline