The enhanced chromatographic resolution associated with Ultra Performance Liquid Chromatography has been demonstrated for peptide mapping (Mazzeo, et al., BioPharm.). The technique improves resolution by a factor of three or more. In addition, the surface chemistry of the BEH Technology used in UPLC has proven especially advantageous for peptide mapping. Good retention and peak shape are observed with either TFA or formic acid as a modifier. These chromatographic characteristics will be useful for synthetic peptides, but there are additional, special requirements. With peptide mapping, the relevant sample components represent a very wide range of chemical and physical properties. Since the map must accommodate all of these components, long, shallow gradients are used. In contrast, synthetic peptides involve a single structure with the contaminants all being closely related structures. It is, therefore, reasonable for the analytical method to be a segmented gradient that is very shallow at the point where the product elutes. Steep gradients can be used to reduce runtime during regeneration and re-equilibration. UPLC should be especially useful for providing the high resolution and high throughput analyses desired for assessing the purity of synthetic peptides. The analytical conditions used in these experiments could also predict the conditions for purifying the peptide if the chemistry was matched in a larger scale column. These experiments test and demonstrate this process with a 23-residue synthetic peptide.