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This method provides a technique for large-scale protein identification using existing one-dimensional HPLC systems . In a recent study, a mixed-mode reversed-phase/weak anion-exchange matrix was used for the separation and purification of peptides . In this paper, a novel material was developed that contains two distinct binding domains, a lipophilic alkyl chain for hydrophobic interactions with lipophilic moieties of the solute, such as in the reversed-phase chromatography, and a cationic site for anion-exchange chromatography with oppositely charged solutes, which also enables repulsive ionic interactions with positively charged functional groups.
That platform exhibited improved sequence coverage and significant shortening of work time . All recent insights in the field of multidimensional peptide separation are described in reviews by Sandra et al.  and Gao et al. . 1 Separation of Amino Acids, Peptides, and Proteins… 19 Fig. 3 A selection of on- and off-line two-dimensional combinations employing SCX (a–g) or RPLC (h) in the first, and RPLC in the second dimension. (a) Biphasic MudPIT [59, 60], (b) triphasic MudPIT , (c) column switching setup using salt steps , (d) and (e) column switching setups employing a linear gradient in the first dimension [63, 64], (f) column switching setup utilizing two second dimension columns, (g) automated off-line setup.
Strength of the interaction between stationary phase and the analyte can be controlled by changing the ionic strength of the solution. Also, ionic properties of ionizable functional groups by pH titration of the stationary phase or the analyte can be controlled, allowing great variability in the design of IE experiments. Strong ion exchangers bear functional groups that are always ionized, over a wide range of pH values. They are typically used to retain and separate weak acids or bases. These weak ions may be eluted by displacement with ions that are more strongly attracted to the stationary phase exchange sites (so-called salt elution).