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DNA/HSA interaction and nuclease activity of an iron(III) amphiphilic sulfonated corrole.
- Source :
- Luminescence: Journal of Biological & Chemical Luminescence; Nov2015, Vol. 30 Issue 7, p1045-1054, 10p
- Publication Year :
- 2015
-
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<superscript>4</superscript> M<superscript>-1</superscript>. 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]
Details
- Language :
- English
- ISSN :
- 15227235
- Volume :
- 30
- Issue :
- 7
- Database :
- Complementary Index
- Journal :
- Luminescence: Journal of Biological & Chemical Luminescence
- Publication Type :
- Academic Journal
- Accession number :
- 110451753
- Full Text :
- https://doi.org/10.1002/bio.2857