Surface functionalization and biomolecule immobilization using plasma-generated free radicals on polypropylene

• Published in: Polymer bulletin (Berlin, Germany) Germany), 2010-07, Vol.65 (3), p.293-308
• Main Authors: de Jesús Martínez-Gómez, Alvaro, Manolache, Sorin O., Young, Raymond A., Denes, Ferencz S.
• Format: Article
• Language: English
• Subjects: Applied sciences; Argon; Biological and medical sciences; Biomolecules; Biotechnology; Characterization and Evaluation of Materials; Chemistry; Chemistry and Materials Science; Chloride; Chymotrypsin; Coating, metallization, dyeing; Complex Fluids and Microfluidics; Computer simulation; Diamines; Enzymes; Exact sciences and technology; Free radicals; Fundamental and applied biological sciences. Psychology; High density polyethylenes; Immobilization; Immobilization of enzymes and other molecules; Immobilization techniques; Machinery and processing; Methods. Procedures. Technologies; Nitric oxide; Organic Chemistry; Original Paper; Oxygen plasma; Physical Chemistry; Plasma; Plastics; Polyethylene; Polymer industry, paints, wood; Polymer Sciences; Polymers; Polypropylene; Soft and Granular Matter; Spectrum analysis; Stainless steel; Substrates; Sulfur; Sulfur dioxide; Technology of polymers; Vapor phases
• ISSN: 0170-0839; 1436-2449
• DOI: 10.1007/s00289-010-0258-1

In this study are presented evidences for the functionalization of polypropylene surfaces accomplished in a sequential process: argon- or oxygen-plasma enhanced generation of free radical sites on polypropylene surfaces was followed by “in situ” gas phase derivatization in the absence of plasma using ethylene diamine, or propylene diamine; and an “in situ”, gas phase derivatization using oxallyl chloride or “ex situ” derivatization in the presence of glutaraldehyde. The free radicals’ presence on the plasma-exposed polypropylene surfaces was confirmed using “ in situ ” sulfur dioxide or nitric oxide labeling techniques. It was shown that the free radical sites readily react under “in situ” conditions with the stable chain-precursor components and generate the desired spacer-chain molecules revealed by ESCA analysis. Functionalized polypropylene substrates were used for immobilization of α-chymotrypsin in the presence of spacer-chain molecules. The activity of the immobilized α-chymotrypsin was found to be comparable to the activity of the free enzyme when the spacer molecules have been used.