A novel, neutral hydroxylated octadecyl acrylate monolith with fast electroosmotic flow velocity and its application to the separation of various solutes including peptides and proteins in the absence of electrostatic interactions.
A neutral hydroxylated octadecyl monolith (ODM-OH) for reversed-phase capillary electrochromatography has been developed. The ODM-OH was prepared by the in situ polymerization of octadecyl acrylate and pentaerythritol triacrylate (PETA) in a ternary porogenic solvent. Pentaerythritol triacrylate possesses a hydroxyl functional group, which imparts the monolith with a hydrophilic group, thus the acronym ODM-OH. The ODM-OH column exhibited cathodal EOF over a wide range of pH and ACN concentration in the mobile phase despite the fact that it was devoid of any fixed charges. This ODM-OH monolith exhibited stronger EOF than its counterpart the ODM made from the in situ polymerization of octadecyl acrylate and trimethylolpropane trimethacrylate. Similar to ODM, it is believed that the EOF was due to the adsorption of ions from the mobile phase onto the surface of the monolith thus imparting the neutral monolithic column the zeta potential necessary to support the EOF. The higher EOF exhibited by ODM-OH was due to the presence of polar OH groups on its surface, which would favor stronger adsorption of ions from the mobile phase. The wide applications of the neutral ODM-OH column were demonstrated in the separation of a wide range of small and large solutes. As a typical result, the ODM-OH was able to separate proteins quite rapidly yielding 200,000 plates/m.
Department of Chemistry, Oklahoma State University, Stillwater, OK 74075, USA.
Samuel
S
Karenga
Ziad
Z
El Rassi
D000097:Acetonitriles; D000179:Acrylates / Q000737:chemistry*; D053801:Capillary Electrochromatography / Q000295:instrumentation* / Q000379:methods; D053841:Electroosmosis; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D009113:Muramidase; D010446:Peptide Fragments / Q000302:isolation & purification*; D010449:Peptide Mapping / Q000379:methods; D011084:Polycyclic Aromatic Hydrocarbons / Q000302:isolation & purification; D058105:Polymerization; D011409:Propylene Glycols / Q000737:chemistry*; D055672:Static Electricity; D014357:Trypsin
D000097:Acetonitriles; D000179:Acrylates; D010446:Peptide Fragments; D011084:Polycyclic Aromatic Hydrocarbons; D011409:Propylene Glycols; C513222:poly(octadecylacrylate); C421864:hen egg lysozyme; D009113:Muramidase; D014357:Trypsin; C027992:pentaerythrityl triacrylate; C032159:acetonitrile