title: Mixed ligand monolithic columns for reversed-phase capillary electrochromatography via hydrophobic and π interactions.
abstract: Novel mixed ligand monoliths (MLM) for capillary electrochromatography (CEC) of a wide range of solutes differing in both polarity and size were introduced. The MLM capillary columns were based on the different compositions of octadecyl acrylate (ODA) and 2-naphthyl methacrylate (NAPM) monomers in the presence of trimethylolpropane trimethacrylate (TRIM) crosslinker and a ternary porogenic solvent made up of cyclohexanol, ethylene glycol, and water. As expected, the magnitude of the electroosmotic flow (EOF) changed with the composition of the MLM. As the percent of the monomer ODA in the polymerization mixture was increased, the EOF increased to a maximum at 50-mol% ODA and then leveled off at 75-mol% and 100-mol% ODA, an indication that the ODA ligand in general exhibited a higher binding for the mobile-phase ions than the NAPM ligand. This is due to the fact that the ODA is an acrylate-based monomer, whereas the NAPM is a methacrylate-based monomer. While ODA provided solely nonpolar interactions, NAPM exhibited both nonpolar and π interactions with certain solutes. It was found out that columns with a given composition of both ligands yielded a unique selectivity for a given set of solutes that was not matched by columns made by either ODA or NAPM alone. Several test mixtures were used in the evaluation of the MLM columns including polycyclic aromatic hydrocarbons, alkyl phenyl ketones, nitroalkanes, alkylbenzenes, toluene derivatives, peptides, and proteins. Peptide mapping of the tryptic digest of the standard lysozyme protein was also studied.
authors.affiliation: Department of Chemistry, Oklahoma State University, Stillwater, OK, USA.
authors.forename: Samuel
authors.initials: S
authors.lastname: Karenga
authors.forename: Ziad El
authors.initials: ZE
authors.lastname: Rassi
mesh_terms: D000179:Acrylates / Q000737:chemistry; D053801:Capillary Electrochromatography / Q000295:instrumentation* / Q000379:methods*; D053841:Electroosmosis; D057927:Hydrophobic and Hydrophilic Interactions; D007526:Isoelectric Point; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D010449:Peptide Mapping; D011084:Polycyclic Aromatic Hydrocarbons / Q000737:chemistry; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
chemical_list: D000179:Acrylates; D010446:Peptide Fragments; D011084:Polycyclic Aromatic Hydrocarbons; D011506:Proteins; D014357:Trypsin