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To understand the extent of the cross-linking of proteins by the bifunctional reagent p-NN'-phenylenebismaleimide, a quantitative study of competing reactions has been undertaken. The two reactive maleimide rings of the bismaleimide are hydrolysed in mildly alkaline aqueous solutions much more rapidly than is the single maleimide ring of the monofunctional analogue N-ethylmaleimide. The kinetics of hydrolysis are second-order, depending on both imide and hydroxyl ion concentration in the pH range 8-10. The hydrolysis of the first imide ring of the bismaleimide is more rapid than the second, with second-order rate constants of 1600 M-1 . s-1 and 500 M-1 . s-1 respectively, at 25 degrees C. The half-times for hydrolysis of the first and second imide rings at pH 9.0 are therefore only 43s and 140s. Because it renders the maleimide ring unreactive towards cysteine, this rapid hydrolysis can limit the extent of cross-linking of proteins by the bismaleimide.

Hydrolysis of p-NN′-phenylenebismaleimide and its adducts with cysteine. Implications for cross-linking of proteins