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113, with Fig. 11 (bottom) representing a summary of what may be achieved when manipulating cation-exchange column selectivity to separate peptides based on a mixed-mode hydrophilic and ionic interaction mechanism. , acetonitrile, to the mobile-phase buffers. Zhu e t al. it3 noted that as the level of acetonitrile was raised from 10 to 90% (in 10% steps), the separation process (linearly increasing gradients of sodium perchlorate with the same level of acetonitrile in both buffers) became increasingly mixed-mode (hydrophilic and ionic interactions), with HILIC interactions becoming dominant at high acetonitrile concentrations.

05% TFA in acetonitrile; flow rate, 1 ml/min; room temperature. The sequence of the peptide analogs is Ac-Gly-X-X(Leu)~-(Lys)2-amide, where position X is occupied by Trp (SW) or Phe (SF). Ac, N'~-Acetyl; amide, C~-amide. (From Ref. ) synthetic peptide analogs were designed to have high potential for forming amphipathic oe helices in a hydrophobic environment such as those characteristic of RP-HPLC. The hydrophobic face of the helix (the preferred binding domain) would be expected to interact with the hydrophobic stationary phase.

J. 1. Chromatogr. 499, 177 (1990). -Y. Zhu, C. T. Mant, and R. S. Hodges, J. Chromatogr. 548, 13 (1991). [11 ANALYSIS OF PEPTIDES BY H P L C 45 the charged character of a cation-exchange sorbent would confer on it considerable hydrophilic character, such a column should be examined for possible peptide separations by HILIC. Classic examples of this approach may be found in Ref. 113, with Fig. 11 (bottom) representing a summary of what may be achieved when manipulating cation-exchange column selectivity to separate peptides based on a mixed-mode hydrophilic and ionic interaction mechanism.

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