A method for preparing, in the internal volume of at least one channel, a monolithic support on which uranyl cations are immobilised. The method comprises: (a) activating the inner surface of the channel(s); (b) introducing, into the internal volume of the channel(s), a polymerisation solution comprising: a monomer comprising a phosphate group, at least one crosslinking agent, several solvents, and a radical polymerisation initiator; (c) polymerising the polymerisation solution; (d) rinsing the monolithic support obtained in step (c); and (e) contacting the monolithic support previously rinsed, with a solution comprising uranyl cations. A method for capturing proteins that selectively bind uranium by means of a monolithic support prepared by the above-mentioned method, as well as to a method for recovering proteins that selectively bind uranium with the capture method.

Provided is a separation method for amine, the separation method including performing liquid chromatography, wherein a separating agent in which a ligand having a crown ether-like cyclic structure is supported on a carrier is used as a stationary phase, and wherein a mobile phase contains an aqueous solution of at least one salt of a hydrophobic anion selected from the group consisting of a salt of a chaotropic anion and a salt of a hydrophobic organic acid.

The present invention provides novel chromatographic materials, e.g., for chromatographic separations, processes for its preparation and separations devices containing the chromatographic material; separations devices, chromatographic columns and kits comprising the same; and methods for the preparation thereof. The chromatographic materials of the invention are chromatographic materials comprising having a narrow particle size distribution.

Spike particles are disclosed including a core and a plurality of spikes attached to and extending from a core surface. The core may be nonporous, superficially porous, or porous. The plurality of spikes may be nonporous or superficially porous. Superficially porous spike particles are disclosed including a porous spike particle shell disposed over a nonporous spike particle. A method for forming the spike particles is disclosed including mixing a dispersed aqueous phase having a plurality of core particles, a water emulsion drop stabilizer, and a catalyst with a continuous oil phase having an organic solvent, polyvinylpyrrolidone, and a silane precursor to form a water-in-oil emulsion system, which is reacted without stirring to form the plurality of chromatographic spike particles. A chromatographic separation device is disclosed including the spike particles, which are randomly packed in the chromatographic separation device and have an external porosity ranging from about 0.4 to about 0.9.

Spike particles are disclosed including a core and a plurality of spikes attached to and extending from a core surface. The core may be nonporous, superficially porous, or porous. The plurality of spikes may be nonporous or superficially porous. Superficially porous spike particles are disclosed including a porous spike particle shell disposed over a nonporous spike particle. A method for forming the spike particles is disclosed including mixing a dispersed aqueous phase having a plurality of core particles, a water emulsion drop stabilizer, and a catalyst with a continuous oil phase having an organic solvent, polyvinylpyrrolidone, and a silane precursor to form a water-in-oil emulsion system, which is reacted without stirring to form the plurality of chromatographic spike particles. A chromatographic separation device is disclosed including the spike particles, which are randomly packed in the chromatographic separation device and have an external porosity ranging from about 0.4 to about 0.9.

The invention relates to poly-amide bonded hydrophilic interaction chromatography (HILIC) stationary phases and novel HILIC methods for use in the characterization of large biological molecules modified with polar groups, known to those skilled in the art as glycans. The invention particularly provides novel, poly-amide bonded materials designed for efficient separation of large biomolecules, e.g. materials having a large percentage of larger pores (i.e. wide pores). Furthermore, the invention advantageously provides novel HILIC methods that can be used in combination with the stationary phase materials described herein to effectively separate protein and peptide glycoforms by eliminating previously unsolved problems, such as on-column aggregation of protein samples, low sensitivity of chromatographic detection of the glycan moieties, and low resolution of peaks due to restricted pore diffusion and long intra/inter-particle diffusion distances.

The invention relates to poly-amide bonded hydrophilic interaction chromatography (HILIC) stationary phases and novel HILIC methods for use in the characterization of large biological molecules modified with polar groups, known to those skilled in the art as glycans. The invention particularly provides novel, poly-amide bonded materials designed for efficient separation of large biomolecules, e.g. materials having a large percentage of larger pores (i.e. wide pores). Furthermore, the invention advantageously provides novel HILIC methods that can be used in combination with the stationary phase materials described herein to effectively separate protein and peptide glycoforms by eliminating previously unsolved problems, such as on-column aggregation of protein samples, low sensitivity of chromatographic detection of the glycan moieties, and low resolution of peaks due to restricted pore diffusion and long intra/inter-particle diffusion distances.

A relatively fast, inexpensive, and non-destructive method for separation and isolation of biologically active nanoparticles is described. Methods include the use of solid phase separation medis such as channeled fibers in a hydrophobic interaction chromatography (HIC) protocol to isolate biologically active nanoparticles from other components of a mixture. Biologically active nanoparticles can include natural nanoparticles (e.g., exosomes, lysosomes, virus particles) as well as synthetic nanoparticles (liposomes, genetically modified virus particles, etc.)

A wash buffer comprising a surfactant for use in affinity and cation exchange chromatography to purify proteins of interest from protein aggregates and to remove and/or inactivate viruses. When used during affinity or cation exchange chromatography for the purification of a protein of interest, such as an antibody, the wash buffer significantly improves viral clearance from the preparation, while also reducing the levels of host cell proteins and protein aggregates. Following affinity or cation exchange chromatography with the wash buffer, the protein of interest may be further purified using other chromatography and filtration operations.

A wash buffer comprising a surfactant for use in affinity and cation exchange chromatography to purify proteins of interest from protein aggregates and to remove and/or inactivate viruses. When used during affinity or cation exchange chromatography for the purification of a protein of interest, such as an antibody, the wash buffer significantly improves viral clearance from the preparation, while also reducing the levels of host cell proteins and protein aggregates. Following affinity or cation exchange chromatography with the wash buffer, the protein of interest may be further purified using other chromatography and filtration operations.