Abstract
An optimized, generally applicable mobile and stationary phase system is identified for the hydrophobic high-performance liquid chromatography (HPLC) of a wide variety of peptides. This reversed-phase system is arrived at as a result of an investigation in which endcapped and non-endcapped, chemically bonded, silicabased supports are compared in terms of their effect on the elution properties of the peptide solutes. Among the peptide solutes included in the study are enkephalins, neurotensins, angiotensins, oxytocin, phenylalanine homopolymers, and products of enzymatic digestion. Some of the features of the optimized phase system are reduced band broadening, improved peak symmetry, excellent resolution, low UV absorbance and volatility of the mobile phase. The retention data that are obtained aid in defining the mechanistic influence that residual silanols have on the elution behavior of peptides chromatographed under hydrophobic HPLC conditions.
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