title: Reversed-phase liquid chromatography of proteins and peptides using multimodal copolymer-encapsulated silica.
abstract: Multimodal copolymer-encapsulated particles for liquid chromatography were prepared by bonding 1-octadecene and unsaturated carboxylic acids on silica particles (5 microm diameter, 300 A pores) for liquid chromatography of proteins. These multimodal copolymer-encapsulated particles can provide both hydrophobic and hydrogen bonding interactions with polar compounds. The chromatographic performance of these multimodal copolymer-encapsulated particles for peptide and protein separations was evaluated under reversed-phase conditions. Compared with typical C8-bonded silica, polymer-encapsulated particles were more stable in acidic mobile phases and provided better recoveries, especially for large proteins (Mr>0.5 x 10(6)). Totally hydrophobic polymer-encapsulated particles were found to produce broad peaks for proteins, and significant improvements were observed by introducing hydrophilic groups (-COOH) onto the polymer-encapsulated surface to form a multimodal phase. For the reversed-phase liquid chromatography of peptides and proteins, improved selectivity and increased solute retention were found using the multimodal polymer-encapsulated particles. More peaks were resolved for the separation of complex peptide mixtures such as protein digests using the multimodal polymer-encapsulated particles as compared to totally hydrophobic polymer-encapsulated particles.
authors.affiliation: Department of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602-5700, USA.
authors.forename: Y
authors.initials: Y
authors.lastname: Shen
authors.forename: X
authors.initials: X
authors.lastname: Shao
authors.forename: K
authors.initials: K
authors.lastname: O'Neill
authors.forename: J S
authors.initials: JS
authors.lastname: Bradshaw
authors.forename: M L
authors.initials: ML
authors.lastname: Lee
mesh_terms: D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D010455:Peptides / Q000032:analysis*; D011108:Polymers; D011506:Proteins / Q000032:analysis*; D012822:Silicon Dioxide; D013056:Spectrophotometry, Ultraviolet
chemical_list: D010455:Peptides; D011108:Polymers; D011506:Proteins; D012822:Silicon Dioxide