Abstract
CE is used to measure the electrophoretic mobility of low molecular mass oligo-L-lysines (n 51-8) in aqueous LiH2PO4 buffer, BGE, at pH 2.5 over a range of temperatures (25-501C) and ionic strengths (10-100 mM). Mobilities are corrected for Joule heating and under the conditions of the experiment, interaction of the peptides with the capillary walls can be ignored. A ''coarse grained'' bead modeling methodology (BMM) (H. Pei et al., J. Chromatogr. A 2009, 1216, 1908-1916) is used to model the mobilities. This model partially accounts for peptide conformation as well as the assumed form of its secondary structure. For highly charged oligolysines, it is necessary to properly account for the relaxation effect. In the present study, the BMM approach tends to overestimate oligolysine mobility and that effect tends to increase with increasing ionic strength and peptide length. It is proposed that association between the oligolysines and buffer components (H2PO4 in this case) that go beyond classical electrostatic interactions are responsible for this discrepancy. A simple binding model is introduced that illustrates how this association can reconcile model and experiment.