Abstract
Maleimide reagents have been examined for a potential use in the cross-linking of amino and thiol groups in proteins. The adducts obtained by reaction of N-ethylmaleimide or of N-(4-dimethyl-3,5-dinitroaminophenyl)maleimide with cysteine, homocysteine, and glutathione were prepared and the rates of reaction of the imide rings with water and with amino groups were studied. In the cysteine—maleimide addition products, where amino and thiol groups are located in positions sterically favourable for cross-linking, intramolecular aminolysis occurs readily. In contrast, the amino group of the homocysteine and glutathione adducts is comparatively stable.
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