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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 K(b) = 1.05 × 10(5) M(−1). TCPC also displayed good pho...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6274405/ https://www.ncbi.nlm.nih.gov/pubmed/26729089 http://dx.doi.org/10.3390/molecules21010054 |
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author | Na, Ning Zhao, Da-Qiang Li, Heng Jiang, Nan Wen, Jin-Yan Liu, Hai-Yang |
author_facet | Na, Ning Zhao, Da-Qiang Li, Heng Jiang, Nan Wen, Jin-Yan Liu, Hai-Yang |
author_sort | Na, Ning |
collection | PubMed |
description | 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 K(b) = 1.05 × 10(5) M(−1). TCPC also displayed good photonuclease activity, which involves singlet oxygen species ((1)O(2)). The binding constant between TCPC and human serum albumin (HSA) is K(A) = 2.24 × 10(5) 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. |
format | Online Article Text |
id | pubmed-6274405 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-62744052018-12-28 DNA Binding, Photonuclease Activity and Human Serum Albumin Interaction of a Water-Soluble Freebase Carboxyl Corrole Na, Ning Zhao, Da-Qiang Li, Heng Jiang, Nan Wen, Jin-Yan Liu, Hai-Yang Molecules Article 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 K(b) = 1.05 × 10(5) M(−1). TCPC also displayed good photonuclease activity, which involves singlet oxygen species ((1)O(2)). The binding constant between TCPC and human serum albumin (HSA) is K(A) = 2.24 × 10(5) 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. MDPI 2015-12-31 /pmc/articles/PMC6274405/ /pubmed/26729089 http://dx.doi.org/10.3390/molecules21010054 Text en © 2016 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons by Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Na, Ning Zhao, Da-Qiang Li, Heng Jiang, Nan Wen, Jin-Yan Liu, Hai-Yang DNA Binding, Photonuclease Activity and Human Serum Albumin Interaction of a Water-Soluble Freebase Carboxyl Corrole |
title | DNA Binding, Photonuclease Activity and Human Serum Albumin Interaction of a Water-Soluble Freebase Carboxyl Corrole |
title_full | DNA Binding, Photonuclease Activity and Human Serum Albumin Interaction of a Water-Soluble Freebase Carboxyl Corrole |
title_fullStr | DNA Binding, Photonuclease Activity and Human Serum Albumin Interaction of a Water-Soluble Freebase Carboxyl Corrole |
title_full_unstemmed | DNA Binding, Photonuclease Activity and Human Serum Albumin Interaction of a Water-Soluble Freebase Carboxyl Corrole |
title_short | DNA Binding, Photonuclease Activity and Human Serum Albumin Interaction of a Water-Soluble Freebase Carboxyl Corrole |
title_sort | dna binding, photonuclease activity and human serum albumin interaction of a water-soluble freebase carboxyl corrole |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6274405/ https://www.ncbi.nlm.nih.gov/pubmed/26729089 http://dx.doi.org/10.3390/molecules21010054 |
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