The electron transfer reactivity of kaempferol and its interaction with amino acid residues

In this work, the electron transfer reactivity of kaempferol was studied and the interaction in vivo between kaempferol and protein was simulated. Dimethylsulfoxide (DMSO) as an aprotic solvent was employed to simulate the specific environment. Various residues of amino acids were used to study the effect of the amino acids in the active site of protein on the electron transfer reactivity of kaempferol. Experimental results revealed that the redox activity of kaempferol was different in aprotic medium DMSO from that in water, and a new redox process was further found. Of all the residues tested, nitrogenous nucleophile, for example, imidazole, was observed to be able to facilitate the electron transfer of kaempferol, and the mechanism was also proposed. This work might provide a simple model to study the electron transfer reactivity of some small active organic molecules, especially medicines, in specific environment, which might approach a more accurate understanding of the activity of some medicines in vivo.