Protein‐reactive, molded polystyrene surfaces having applications to immunoassay formats

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Abstract
Injection‐molded polystyrene surfaces were chemically modified rendering them protein reactive. The process involves chlorosulfonation of the aromatic ring, sulfonamide formation with excess di‐ and triamines, and reaction of the residual pendant amines with various bifunctional molecules. Surfaces possessing pendant bromoacetyl, iodoacetyl, fluorodinitrophenyl, and trimellitic anhydride were prepared and can exhibit up to ten times more protein immobilization capability compared to unfunctionalized polystyrene, where the coupling takes place presumably via hydrophobic interaction.

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