Capillary-channeled Polymer Fibers as Stationary Phases for Protein Chromatography

The affinity ligand quality of the triazine dye, cibacron blue, toward serum albumin has been well studied [64-68]. By immobilizing the ligand to a stationary phase, affinity separations can be performed in order to remove bulk albumin from serum samples. This decrease in albumin concentration may serve as a direct advantage for proteomics as large amounts of serum albumin hinder the study of low abundance proteins of interest [69]. Capillary-channeled polymer (CCP) fiber columns have shown promise in protein separations as they demonstrate low backpressures ideal for viscous protein samples, virtually nonporous surfaces with respect to proteins which reduce van Deemter C-term effects, and high mass transfer rates to increase solute interactions at the stationary phase surface. Combining these attributes with the specificity of cibacron blue would generate a useful depletion column that could be used in spin-down or column formats. Nylon’s terminal amine can react directly with the chloride moiety of the triazine dye covalently. Complementarily, head-groupmodified PEG-lipids can be used on polypropylene (PP) fibers for the same end goal [62, 63]. While this may be a useful study, results were far exceeded by commercial and previous publications [64, 67-72].