title: Polymeric strong cation-exchange monolithic column for capillary liquid chromatography of peptides and proteins.
abstract: A strong cation-exchange (SCX) monolithic stationary phase was prepared in 75 microm id capillaries by direct in situ polymerization of sulfopropyl methacrylate and polyethylene glycol diacrylate in a ternary porogen system consisting of methanol, cyclohexanol, and water. The resulting monolith exhibited good dynamic binding capacity, fast kinetic adsorption of proteins, and high permeability. The monolith had a dynamic binding capacity of approximately 52 mg/mL of column volume for lysozyme and cytochrome C. The monolith was evaluated for SCX capillary LC of synthetic peptides, natural peptides, and protein standards. Fast separation of proteins was achieved in less than 4 min. The average peak capacity for peptides was 28 using a relatively steep gradient when hydrophobic interactions were suppressed with 40% acetonitrile.
authors.affiliation: Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT, USA.
authors.forename: Xin
authors.initials: X
authors.lastname: Chen
authors.forename: H Dennis
authors.initials: HD
authors.lastname: Tolley
authors.forename: Milton L
authors.initials: ML
authors.lastname: Lee
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002412:Cations / Q000737:chemistry*; D002852:Chromatography, Ion Exchange / Q000295:instrumentation* / Q000379:methods; D006801:Humans; D007475:Ion Exchange Resins / Q000737:chemistry*; D008689:Methacrylates / Q000737:chemistry; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010455:Peptides / Q000302:isolation & purification*; D011092:Polyethylene Glycols / Q000737:chemistry; D011108:Polymers / Q000737:chemistry*; D011506:Proteins / Q000302:isolation & purification*
chemical_list: D002412:Cations; D007475:Ion Exchange Resins; D008689:Methacrylates; D010455:Peptides; D011108:Polymers; D011506:Proteins; C437167:poly(ethylene glycol)diacrylate; D011092:Polyethylene Glycols