Sunlight-mediated activation of an inert polymer surface for covalent immobilization of a protein.
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.
Nahar
Pradip
P
Institute of Genomics and Integrative Biology (CSIR), Delhi University Campus, Mall Road, Delhi 110007, India. p_nahar@hotmail.com
Naqvi
Azmi
A
Basir
Seemi Farhat
SF
D001386:Azides / Q000737:chemistry / Q000528:radiation effects*; D004800:Enzymes, Immobilized / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry; D009578:Nitrobenzenes / Q000737:chemistry / Q000528:radiation effects*; D010777:Photochemistry / Q000379:methods*; D010969:Plastics / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry; D013472:Sunlight; D014466:Ultraviolet Rays
C492759:1-fluoro-2-nitro-4-azidobenzene; D001386:Azides; D004800:Enzymes, Immobilized; D009578:Nitrobenzenes; D010969:Plastics; D011506:Proteins; D006735:Horseradish Peroxidase