Sunlight-mediated activation of an inert polymer surface for covalent immobilization of a protein

• Published in: Analytical biochemistry Vol. 327; no. 2; pp. 162 - 164
• Main Authors: Nahar, Pradip, Naqvi, Azmi, Basir, Seemi Farhat
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15.04.2004
• Subjects: Azides - chemistry; Azides - radiation effects; Enzymes, Immobilized - chemistry; Horseradish Peroxidase - chemistry; Nitrobenzenes - chemistry; Nitrobenzenes - radiation effects; Photochemistry - methods; Plastics - chemistry; Proteins - chemistry; Sunlight; Ultraviolet Rays
• ISSN: 0003-2697; 1096-0309
• DOI: 10.1016/j.ab.2003.11.030

Polystyrene, polypropylene, and polyethylene surfaces were activated by exposing 1-fluoro-2-nitro-4-azidobenzene coated surface to sunlight. Sunlight intensity of 26,300 lux was found optimum beyond which no appreciable increase in activation was observed. Five-minutes sunlight exposure gave better activated surface than 5 min 365-nm UV light exposure. The efficacy of sunlight-mediated activated surfaces was demonstrated by covalently immobilizing proteins onto them. Horseradish peroxidase when immobilized onto the sunlight-activated surfaces showed more than twofold increase in immobilization than the surface without activation. Thus, sunlight being a versatile, eco-friendly, and clean energy source can be a potential alternative for activation of inert surface for covalent attachment of biomolecule such as protein, DNA, or carbohydrate.