Evidence map›Paper›PMID 27376275›Full record

ArticleInternational journal of molecular sciences2016

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

Zhongjie Xu, Youxun Liu, Sufeng Zhou, Yun Fu, Changzheng Li

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 21 citations in OpenAlex.

  1. Human serum albumin as a copper source for anticancer thiosemicarbazones.Metallomics : integrated biometal science · 2023
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Zhongjie XuCollege of Life Science and Technology, Xinxiang Medical University, Xinxiang 453003, China. xcj029@163.com.
Youxun LiuDepartment of Molecular Biology & Biochemistry, Xinxiang Medical University, Xinxiang 453003, China. liuyouxun@126.com.
Sufeng ZhouDepartment of Molecular Biology & Biochemistry, Xinxiang Medical University, Xinxiang 453003, China. sufengzhou@xxmu.edu.cn.
Yun FuDepartment of Molecular Biology & Biochemistry, Xinxiang Medical University, Xinxiang 453003, China. fuyun9801@163.com.
Changzheng LiDepartment of Molecular Biology & Biochemistry, Xinxiang Medical University, Xinxiang 453003, China. changzhengli@xxmu.edu.cn.
Xinxiang Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AnimalsBinding SitesCattleCell DifferentiationCircular DichroismCoordination ComplexesCopperDNAHep G2 CellsHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsMolecular Docking SimulationNucleic Acid ConformationProtein BindingProtein Structure, Tertiarycalf thymus DNACoordination ComplexesCopperdi-2-pyridylketone-4,4-dimethyl-3-thiosemicarbazoneDNASerum AlbuminThiosemicarbazonesDp44mTfluorescence quenchingmolecular docking

Identifiers

PMID27376275
PMCPMC4964418
OpenAlexW2460999297

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.