Clean Technology 2010

A noble affinity material for peptide and protein

S. Chakraborty, K.-S Lin, D.-F Tai
national dong-hwa university, TW

Keywords: peptides, protein, molecular imprinting, solid-phase extraction, enrichment


We developed two type artificial affinity materials for peptide separation and protein purification. At first, the surface alcohol on cellulose paper was converted to chloride and reacted with ethylene diamine, followed by acrylation. After washing the cellulose with ethanol three times, molecularly imprinted film (MIF) was fabricated with peptide onto modified cellulose paper. Molecularly imprinted polymers were also generated directly without support to compare their extraction characteristics with MIPs coated on cellulose paper (MIFC). In loading ability studies, peptide masses up to 100 µg could be adsorbed onto an MIFC (0.7 cm in diameter). The quantitative analysis of the adsorbed peptide by high-performance liquid chromatography (HPLC)-UV employing RP-18 columns revealed that the affinity constant (Kd) in micromolar range. On a preparative scale, by means of direct-immersion, such obtained MIFC are able to exhibit selectivity, leading eventually to better product qualities. The great capability and reusability of such separation unit should be suitable for the extraction or analysis of biological samples. These MIP-coated cellulose paper was able to isolate low levels of peptide or protein contained in a reaction mixture, despite the presence of appreciable quantities of other peptide fragments.
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