DNA/HSA interaction and nuclease activity of an iron(III) amphiphilic sulfonated corrole

Luminescence : the Journal of Biological and Chemical Luminescence
Yang ZhangHai-Yang Liu

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.

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Citations

Jan 6, 2016·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Ning NaHai-Yang Liu
Oct 21, 2016·Chemical Reviews·Ruijie D TeoHarry B Gray
Jul 14, 2017·Dalton Transactions : an International Journal of Inorganic Chemistry·Zhao ZhangHai-Yang Liu
Jan 4, 2019·Luminescence : the Journal of Biological and Chemical Luminescence·Khyati P ThakorMohan N Patel
Aug 23, 2019·Journal of Biomolecular Structure & Dynamics·Nahid ShahabadiSaba Hadidi

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