The unsaturated carbonyl structure of ACR is a soft electrophile that will preferentially form Michael-type adducts with soft nucleophiles, which in biological systems are sulfhydryl side-chains on cysteine residues.
Thus, we realized that ACR was a soft electrophile that preferentially formed adducts with soft nucleophilic sites on macro-molecules.
We also show how application of the hard and soft, acids and bases (HSAB) theory led to the recognition that the [alpha], [beta]-unsaturated carbonyl structure of ACR is a soft electrophile that preferentially forms covalent bonds with soft nucleophiles.
KEY WORDS: HSAB theory, oxidative stress, protein adducts, soft electrophile, toxic axonopathy, type-2 alkenes, [alpha], [beta]-unsaturated carbonyl derivatives.
As indicated above, soft electrophiles such as ACR preferentially react with soft nucleophiles.