Molecules 2016, 21(1), 54; https://doi.org/10.3390/molecules21010054
DNA Binding, Photonuclease Activity and Human Serum Albumin Interaction of a Water-Soluble Freebase Carboxyl Corrole
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
Received: 30 September 2015 / Revised: 21 December 2015 / Accepted: 24 December 2015 / Published: 31 December 2015
(This article belongs to the Special Issue Tetrapyrroles, Porphyrins and Phthalocyanines)
Abstract
The DNA binding property of 5,10,15-Tris(4-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-TextKeywords:
corrole; DNA; human serum albumin; photonuclease activity
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Na, N.; Zhao, D.-Q.; Li, H.; Jiang, N.; Wen, J.-Y.; Liu, H.-Y. DNA Binding, Photonuclease Activity and Human Serum Albumin Interaction of a Water-Soluble Freebase Carboxyl Corrole. Molecules 2016, 21, 54.
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