DNA/HSA interaction and nuclease activity of an iron(III) amphiphilic sulfonated corrole |
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| Authors: | Yang Zhang Jin‐Yan Wen Mian HR Mahmood Xiang‐Li Wang Biao‐Biao Lv Xiao Ying Hui Wang Liang‐Nian Ji Hai‐Yang Liu |
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| Affiliation: | 1. Department of Chemistry, South China University of Technology, Guangzhou, China;2. Department of Applied Phsics, South China University of Technology, Guangzhou, China;3. State Key Laboratory of Optoelectronics Materials and Technologies, Sun‐Yat Sen University, Guangzhou, China;4. MOE Laboratory of Bioinorganic and Synthetic Chemistry, Sun‐Yat Sen University, Guangzhou, China |
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| Abstract: | The DNA binding of amphiphilic iron(III) 2,17‐bis(sulfonato)‐5,10,15‐tris(pentafluorophenyl)corrole complex (Fe–SC) was studied using spectroscopic methods and viscosity measurements. Its nuclease‐like activity was examined by using pBR322 DNA as a target. The interaction of Fe–SC with human serum albumin (HSA) in vitro was also examined using multispectroscopic techniques. Experimental results revealed that Fe–SC binds to ct‐DNA via an outside binding mode with a binding constant of 1.25 × 104 M–1. This iron corrole also displays good activity during oxidative DNA cleavage by hydrogen peroxide or tert‐butyl hydroperoxide oxidants, and high‐valent (oxo)iron(V,VI) corrole intermediates may play an important role in DNA cleavage. Fe–SC exhibits much stronger binding affinity to site II than site I of HSA, indicating a selective binding tendency to HSA site II. The HSA conformational change induced by Fe–SC was confirmed by UV/Vis and CD spectroscopy. Copyright © 2015 John Wiley & Sons, Ltd. |
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| Keywords: | corrole iron DNA nuclease activity HSA |
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