| STUDY |
DNA-cleaving agents may aid studies on protein radicals A new class of amino acid-based DNA-cleaving agents developed by chemists at Boston College may prove useful in studying the damaging effects of protein radicals generated in cells. Assistant professor Shana O. Kelley, graduate students Kerry P. Mahon Jr. and Erin G. Prestwich, and undergraduate Rodrigo F. Ortiz-Meoz attach a dipeptide containing tryptophan and lysine to thiazole orange, a planar molecule that binds DNA by slipping between base pairs [Chem. Commun., 2003, 1956]. When exposed to visible light, the peptide-intercalator conjugate forms a tryptophan-based peroxyl radical that cleaves DNA. Photoexcitation of the intercalator generates singlet oxygen (1O2) in close proximity to tryptophan, leading to formation of the radical. Conjugates containing tyrosine instead of tryptophan behave similarly. Kelley's team hopes to use the peptide-intercalator conjugates as model systems to study the reactivity of amino acid peroxyl radicals and the dangers such species may pose to cells and their DNA. |
| UPDATE | 07.03 |
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