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Correction published on 16 November 2016, see Int. J. Mol. Sci. 2016, 17(11), 1915.
Letter published on 16 November 2016, see Int. J. Mol. Sci. 2016, 17(11), 1916.
Article

Analysis of the Interaction of Dp44mT with Human Serum Albumin and Calf Thymus DNA Using Molecular Docking and Spectroscopic Techniques

by 1,†, 2,†, 2, 2 and 2,3,*
1
College of Life Science and Technology, Xinxiang Medical University, Xinxiang 453003, China
2
Department of Molecular Biology & Biochemistry, Xinxiang Medical University, Xinxiang 453003, China
3
Henan Collaborative Innovation Center of Molecular Diagnostics and Laboratory Medicine, Xinxiang 453003, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Gregor Drummen
Int. J. Mol. Sci. 2016, 17(7), 1042; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms17071042
Received: 4 May 2016 / Revised: 14 June 2016 / Accepted: 24 June 2016 / Published: 30 June 2016
(This article belongs to the Section Biochemistry)
Di-2-pyridylketone-4,4,-dimethyl-3-thiosemicarbazone (Dp44mT) exhibits significant antitumor activity. However, the mechanism of its pharmacological interaction with human serum albumin (HSA) and DNA remains poorly understood. Here, we aimed to elucidate the interactions of Dp44mT with HSA and DNA using MTT assays, spectroscopic methods, and molecular docking analysis. Our results indicated that addition of HSA at a ratio of 1:1 did not alter the cytotoxicity of Dp44mT, but did affect the cytotoxicity of the Dp44mT-Cu complex. Data from fluorescence quenching and UV-VIS absorbance measurements demonstrated that Dp44mT could bind to HSA with a moderate affinity (Ka = approximately 104 M−1). CD spectra revealed that Dp44mT could slightly disrupt the secondary structure of HSA. Dp44mT could also interact with Ct-DNA, but had a moderate binding constant (KEB = approximately 104 M−1). Docking studies indicated that the IB site of HSA, but not the IIA and IIIA sites, could be favorable for Dp44mT and that binding of Dp44mT to HSA involved hydrogen bonds and hydrophobic force, consistent with thermodynamic results from spectral investigations. Thus, the moderate binding affinity of Dp44mT with HSA and DNA partially contributed to its antitumor activity and may be preferable in drug design approaches. View Full-Text
Keywords: Dp44mT; fluorescence quenching; molecular docking Dp44mT; fluorescence quenching; molecular docking
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MDPI and ACS Style

Xu, Z.; Liu, Y.; Zhou, S.; Fu, Y.; Li, C. Analysis of the Interaction of Dp44mT with Human Serum Albumin and Calf Thymus DNA Using Molecular Docking and Spectroscopic Techniques. Int. J. Mol. Sci. 2016, 17, 1042. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms17071042

AMA Style

Xu Z, Liu Y, Zhou S, Fu Y, Li C. Analysis of the Interaction of Dp44mT with Human Serum Albumin and Calf Thymus DNA Using Molecular Docking and Spectroscopic Techniques. International Journal of Molecular Sciences. 2016; 17(7):1042. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms17071042

Chicago/Turabian Style

Xu, Zhongjie, Youxun Liu, Sufeng Zhou, Yun Fu, and Changzheng Li. 2016. "Analysis of the Interaction of Dp44mT with Human Serum Albumin and Calf Thymus DNA Using Molecular Docking and Spectroscopic Techniques" International Journal of Molecular Sciences 17, no. 7: 1042. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms17071042

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