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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.

Open AccessArticle
Int. J. Mol. Sci. 2016, 17(7), 1042; doi:10.3390/ijms17071042

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

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
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Gregor Drummen
Received: 4 May 2016 / Revised: 14 June 2016 / Accepted: 24 June 2016 / Published: 30 June 2016
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
View Full-Text   |   Download PDF [3441 KB, uploaded 17 November 2016]   |  

Abstract

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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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.

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