CHARACTERIZATION OF A CHIRAL TRIPEPTIDE STATIONARY PHASE FOR THE LIQUID CHROMATOGRAPHIC SEPARATION OF CHIRAL DIPEPTIDES.

Article abstract of DOI:10.1021/ac00280a010

A tripeptide-bonded stationary phase was synthesized by bonding the tripeptide, L-Val-L-Ala-L-Pro, to a reactive silane bonded to silica gel. The retention behavior of several isomeric dipeptides was examined as a function of pH and buffer composition. Although retention behaviors were similar to those reported for the nominally same tripeptide phase prepared in another way, the data indicated that the phases were significantly different. In addition, for the new phase at pH 7. 4, a buffer effect was found in which retentions decreased on going from a phosphate-citrate-chloride (McIlvaine) to phosphate buffer alone, to citrate alone, and to pyrophosphate.