A novel monolithic column for capillary electrochromatographic separation of oligopeptides

作者：Lin Chun Chi; Wang Guan Ren; Liu Chuen Ying^*

来源：Analytica Chimica Acta, 2006, 572(2): 197-204.

DOI：10.1016/j.aca.2006.05.028

• monolithic column
• capillary electrochromatography
• oligopeptides

A monolithic column was prepared using L-phenylalanine as template and a covalent approach through the formation of Schiff base with o-phthalaldehyde (OPA). OPA, allylmercaptan, L-phenylalanine, and triethylamine were stirred at first, then methacrylic acid, 2-vinylpyridine, ethyleneglycoldimethacrylate,alpha,alpha-azobisisobutyronitrile, and 1-propanol were added to the reaction mixture. The resulting material was introduced into a capillary column. Following thermal polymerization, the template was then extracted with a mixture of HCl and methanol. The column was employed for the capillary electrochromatographic separation of oligopeptides. A capillary column of 75 (50) cm x 75 mu m ID with a mobile phase of phosphate buffer (pH 7.0, 40 mM)/methanol (5%, v/v), an applied voltage of + 15 kV, and detection at 214 nm, could baseline separate angiotensin I, angiotensin II, [Sar(1), Thr(8)] angiotensin, oxytocin, vasopressin, tocinoic acid, P-casomorphin bovine, P-casomorphin human, and FMRF amide within 20 min. The separation behavior of the templated polymer was also compared with that of the non-templated polymer. As a result, it can be concluded that the electrochromatographic separation of this set of peptides was mediated by a combination of electrophoretic migration and chromatographic retention involving hydrophobic, hydrogen bonding, electrostatic as well as the Schiff base formation with OPA in the cavity of the templated polymer.

• 出版日期2006-7-21