DNA Binding, Photonuclease Activity and Human Serum Albumin Interaction of a Water-Soluble Freebase Carboxyl CorroleReport as inadecuate




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1

Department of Kidney Transplantation, The Third Affiliated Hospital of Sun Yat-sen University, Guangzhou 510630, China

2

Department of Hepatic Surgery, The Third Affiliated Hospital of Sun Yat-sen University, Guangzhou 510630, China

3

Department of Chemistry, South China University of Technology, Guangzhou 510640, China



These authors contributed equally to this work.





*

Authors to whom correspondence should be addressed.



Academic Editor: Giuseppe Mele

Abstract The DNA binding property of 5,10,15-Tris4-carboxyphenyl corrole TCPC was studied by UV-Visible, fluorescence and circular dichroism CD spectroscopic methods. TCPC can bind to ct-DNA via an outside binding mode with the binding constant of Kb = 1.05 × 105 M−1. TCPC also displayed good photonuclease activity, which involves singlet oxygen species 1O2. The binding constant between TCPC and human serum albumin HSA is KA = 2.24 × 105 M−1 with a simulated binding distance of 2.06 nm. The fluorescence quenching of HSA by TCPC followed a static quenching process. Site marker competitive displacement experiments indicated that warfarin site I is the main binding site. The secondary structure of HSA was changed upon interaction with TCPC, which was confirmed by UV-Visible and CD spectroscopy. View Full-Text

Keywords: corrole; DNA; human serum albumin; photonuclease activity corrole; DNA; human serum albumin; photonuclease activity





Author: Ning Na 1,†, Da-Qiang Zhao 1,†, Heng Li 1, Nan Jiang 2,* , Jin-Yan Wen 3 and Hai-Yang Liu 3,*

Source: http://mdpi.com/



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