l-Histidyl-glycyl-glycyl-l-histidine. Amino-acid structuring of the bleomycin-type pentadentate metal-binding environment capable of efficient double-strand cleavage of plasmid DNA |
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| Institution: | 1. Morsani College of Medicine, Department of Pathology and Cell Biology, University of South Florida, Tampa, FL 33612, United States;2. Department of Cancer Biology and Evolution, H. Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612, United States;3. Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada;4. Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, FL 33620, United States;5. Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, United States;6. USF Health Byrd Alzheimer''s Research Institute, University of South Florida, Tampa, FL 33612, United States;7. Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russian Federation |
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| Abstract: | A tetrapeptide, l-histidyl-glycyl-glycyl-l-histidine (HGGH), was synthesized and the pUC19 plasmid DNA cleaving activity by copper(II) complex of HGGH (Cu(II)?HGGH) was investigated. Cu(II)?HGGH showed bleomycin-like DNA cleaving activity and, at 50 nM, converted a supercoiled DNA efficiently to a linear DNA in the presence of 500 μM H2O2/sodium ascorbate through an oxidative pathway. |
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| Keywords: | Tetrapeptide Copper DNA Cleavage |
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