1. DNA/HSA interaction and nuclease activity of an iron(III) amphiphilic sulfonated corrole.
- Author
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Zhang, Yang, Wen, Jin‐Yan, Mahmood, Mian HR, Wang, Xiang‐Li, Lv, Biao‐Biao, Ying, Xiao, Wang, Hui, Ji, Liang‐Nian, and Liu, Hai‐Yang
- 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 × 10
4 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. [ABSTRACT FROM AUTHOR]- Published
- 2015
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