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

Autor: Yang, Zhang, Jin-Yan, Wen, Mian H R, Mahmood, Xiang-Li, Wang, Biao-Biao, Lv, Xiao, Ying, Hui, Wang, Liang-Nian, Ji, Hai-Yang, Liu
Rok vydání: 2014
Předmět:
Zdroj: Luminescence : the journal of biological and chemical luminescence. 30(7)
ISSN: 1522-7243
Popis: 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.
Databáze: OpenAIRE