DNA/HSA interaction and nuclease activity of an iron(III) amphiphilic sulfonated corrole.
Luminescence
; 30(7): 1045-54, 2015 Nov.
Article
em En
| MEDLINE
| ID: mdl-25736221
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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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Porfirinas
/
Ácidos Sulfônicos
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Tensoativos
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DNA Super-Helicoidal
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Albumina Sérica
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Compostos Férricos
Limite:
Humans
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article