| MECHANISM OF ACTION |
Alkyltins target brain protein dithiol The selective neurotoxicity of certain organotin compounds may stem from their ability to bind to dithiols found in membrane proteins of the central nervous system. Trialkyltin salts were once widely used as antifouling agents in paint and as fungicides for agriculture. Although their use has been banned, concern remains about the possible health effects of residual trialkyltins in the environment. Stannin, a small membrane protein in the brain, was recently shown to mediate the selective neurotoxicity of trimethyltin in mammals. Now, a team led by Gianluigi Veglia, an assistant professor of chemistry at the University of Minnesota, Minneapolis, has figured out how trialkyltins bind to a small piece of this protein that contains a pair of cysteine residues [J. Am. Chem. Soc., 125, 13316 (2003)]. Veglia’s team shows that the peptide’s thiols bind to and dealkylate trialkyltin compounds containing three or fewer carbon atoms per alkyl chain. The structure the peptide assumes with dimethyltin bound (shown with peptide in light blue, cysteine sulfurs in yellow, tin as blue ball, and methyl groups in gray and black ball-and-stick) will soon be published, |
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