Development of porous polymer monoliths for reverse-phase chromatography of proteins.
Abstract
The polymers developed in this project are intended for use as a stationary phase in reverse-phase chromatography of proteins, where the mobile phase is a solution of acetonitrile and a phosphate buffer, 6.6 pH. A full library of pore sizes have been developed ranging from 0.41{micro}m to 4.09 {micro}m; these pore sizes can be determined by the solvent ratio of tetrahydrofuran:methoxyethanol during polymerization. A column that can separate proteins in an isocratic mode would be a vast improvement from the common method of separating proteins through gradient chromatography using multiple solvents. In the stationary phase, the main monomers have hydrophobic tails, lauryl acrylate and steryl acrylate. Separations of small hydrophobic molecules and peptides (trial molecules) have efficiencies of 24,000-33,000 theoretical plates m{sup -1}. The combination of a highly non-polar stationary phase and a mobile phase where the polarity can be controlled provide for excellent separation.
- Authors:
-
- Sandia National Laboratories, Albuquerque, NM
- Publication Date:
- Research Org.:
- Sandia National Laboratories (SNL), Albuquerque, NM, and Livermore, CA (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 918341
- Report Number(s):
- SAND2003-8517
TRN: US200818%%353
- DOE Contract Number:
- AC04-94AL85000
- Resource Type:
- Technical Report
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; ACETONITRILE; ACRYLATES; CHROMATOGRAPHY; MONOMERS; PEPTIDES; PHOSPHATES; PLATES; POLYMERIZATION; POLYMERS; PROTEINS; SOLVENTS
Citation Formats
Shepodd, Timothy J, and Stephens, Christopher P. Development of porous polymer monoliths for reverse-phase chromatography of proteins.. United States: N. p., 2003.
Web. doi:10.2172/918341.
Shepodd, Timothy J, & Stephens, Christopher P. Development of porous polymer monoliths for reverse-phase chromatography of proteins.. United States. https://doi.org/10.2172/918341
Shepodd, Timothy J, and Stephens, Christopher P. 2003.
"Development of porous polymer monoliths for reverse-phase chromatography of proteins.". United States. https://doi.org/10.2172/918341. https://www.osti.gov/servlets/purl/918341.
@article{osti_918341,
title = {Development of porous polymer monoliths for reverse-phase chromatography of proteins.},
author = {Shepodd, Timothy J and Stephens, Christopher P},
abstractNote = {The polymers developed in this project are intended for use as a stationary phase in reverse-phase chromatography of proteins, where the mobile phase is a solution of acetonitrile and a phosphate buffer, 6.6 pH. A full library of pore sizes have been developed ranging from 0.41{micro}m to 4.09 {micro}m; these pore sizes can be determined by the solvent ratio of tetrahydrofuran:methoxyethanol during polymerization. A column that can separate proteins in an isocratic mode would be a vast improvement from the common method of separating proteins through gradient chromatography using multiple solvents. In the stationary phase, the main monomers have hydrophobic tails, lauryl acrylate and steryl acrylate. Separations of small hydrophobic molecules and peptides (trial molecules) have efficiencies of 24,000-33,000 theoretical plates m{sup -1}. The combination of a highly non-polar stationary phase and a mobile phase where the polarity can be controlled provide for excellent separation.},
doi = {10.2172/918341},
url = {https://www.osti.gov/biblio/918341},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Mon Sep 01 00:00:00 EDT 2003},
month = {Mon Sep 01 00:00:00 EDT 2003}
}