期刊
ANNUAL REVIEW OF ANALYTICAL CHEMISTRY
卷 2, 期 -, 页码 387-408出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-anchem-060908-155153
关键词
protein immobilization; phosphopeptide enrichment; protein microarrays; immobilized metal-affinity chromatography; ion exchange; size exclusion
资金
- National Science Foundation [CHE-0616795]
- National Institutes of Health [GM080511]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM080511] Funding Source: NIH RePORTER
This review examines the application of polymer brush-modified flat surfaces, membranes, and beads for protein immobilization and isolation. Modification of porous substrates with brushes yields membranes that selectively bind tagged proteins to give 99% pure protein at capacities as high as 100 mg of protein per cubic centimeter of membrane. Moreover, enrichment of phosphopeptides on brush-modified matrix-assisted laser desorption/ionization (MALDI) plates allows detection and characterization of femtomole levels of phosphopeptides by MALDI, mass spectrometry. Because swollen hydrophilic brushes can resist nonspecific protein adsorption while immobilizing a high density of proteins, they are attractive as substrates for protein microarrays. This review highlights the advantages of polymer brush-modified surfaces over self-assembled monolayers and identifies some research needs in this area.
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