FTIR-ATR spectra of protein A immobilized on to functionalized polypropylene membranes by gaseous plasma of oxygen and of anhydrous ammonia.
Polypropylene membranes were treated in a gaseous plasma of oxygen or anhydrous ammonia, in order to add hydroxyl groups (oxygen plasma) or amino groups (ammonia plasma) on their surfaces. The presence of these functional groups was detected by FTIR-ATR spectrometry. The FTIR-ATR spectrum of free Protein A was recorded and absorption bands for amide I and amide II at 1650 cm-1 and 1552 cm-1 were identified. The surfaces of immobilized Protein A on to hydroxylated polypropylene membranes and on to polypropylene membranes having amino groups, were characterized by FTIR-ATR spectrometry. The presence of amide I and amide II absorption bands confirmed the immobilization of Protein A on to functionalized polypropylene membranes by gaseous plasma modification.
Sipehia
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Artificial Cells and Organs Research Centre, Faculty of Medicine, McGill University, Montreal, Quebec, Canada.
D000641:Ammonia; D008567:Membranes, Artificial; D010100:Oxygen; D011126:Polypropylenes; D013055:Spectrophotometry, Infrared / Q000379:methods; D013205:Staphylococcal Protein A / Q000032:analysis*; D013499:Surface Properties
D008567:Membranes, Artificial; D011126:Polypropylenes; D013205:Staphylococcal Protein A; D000641:Ammonia; D010100:Oxygen