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Molecules, Vol. 21, Pages 54: DNA Binding, Photonuclease Activity and Human Serum Albumin Interaction of a Water-Soluble Freebase Carboxyl Corrole

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.

Authors:   Na, Ning ; Zhao, Da-Qiang ; Li, Heng ; Jiang, Nan ; Wen, Jin-Yan ; Liu, Hai-Yang
Journal:   Molecules
Volume:   21
edition:   1
Year:   2015
Pages:   54
DOI:   10.3390/molecules21010054
Publication date:   31-Dec-2015
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