Evidence map›Paper›PMID 30387064›Full record

ArticleEnvironmental science and pollution research international2019

A biophysical probe on the binding of 2-mercaptothioazoline to bovine hemoglobin.

Luyi Zou, Xiaoyue Zhang, Mingying Shao, Ruirui Sun, Yuting Zhu, Binbin Zou, Zhenxing Huang, He Liu, Yue Teng

Abstract read
PubMed Publisher
In one paragraph

Article in Environmental science and pollution research international, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 50% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Luyi ZouSchool of Environmental and Civil Engineering, Jiangnan University, 1800# Lihu Avenue, Wuxi, 214122, People's Republic of China.
Xiaoyue ZhangSchool of Environmental and Civil Engineering, Jiangnan University, 1800# Lihu Avenue, Wuxi, 214122, People's Republic of China.
Mingying ShaoSchool of Environmental and Civil Engineering, Jiangnan University, 1800# Lihu Avenue, Wuxi, 214122, People's Republic of China.
Ruirui SunSchool of Environmental and Civil Engineering, Jiangnan University, 1800# Lihu Avenue, Wuxi, 214122, People's Republic of China.
Yuting ZhuSchool of Environmental and Civil Engineering, Jiangnan University, 1800# Lihu Avenue, Wuxi, 214122, People's Republic of China.
Binbin ZouSchool of Environmental and Civil Engineering, Jiangnan University, 1800# Lihu Avenue, Wuxi, 214122, People's Republic of China.
Zhenxing HuangSchool of Environmental and Civil Engineering, Jiangnan University, 1800# Lihu Avenue, Wuxi, 214122, People's Republic of China.
He LiuSchool of Environmental and Civil Engineering, Jiangnan University, 1800# Lihu Avenue, Wuxi, 214122, People's Republic of China.
Yue TengSchool of Environmental and Civil Engineering, Jiangnan University, 1800# Lihu Avenue, Wuxi, 214122, People's Republic of China. tengyue@jiangnan.edu.cn.
Jiangnan University · CN

Funding

China Postdoctoral Science Foundation 2016M590411Jiangsu Province Postdoctoral Research Funding Scheme 1601230CNational Nature Science Foundation of China 21307043National Nature Science Foundation of China 21506076National Nature Science Foundation of China 21577083National Science and Technology Major Project 2017ZX07203001
6 · The paper itself

Abstract

2-Mercaptothiazoline (MTZ) is broadly present in daily use as an antifungal reagent, a brightening agent, and a corrosion inhibitor. MTZ is potentially harmful for human health. Although the toxic effects of MTZ on experimental animals have been reported, the effects of MTZ on the proteins in the circulatory system at the molecular level have not been identified previously. Here, we explored the interaction of MTZ with bovine hemoglobin (BHb) in vitro using multiple spectroscopic techniques and molecular docking. In this study, the binding capacity, acting force, binding sites, molecular docking simulation, and conformational changes were investigated. MTZ quenched the intrinsic emission of BHb via the static quenching process and could spontaneously bind with BHb mainly through van der Waals forces and hydrogen bond. The computational docking visualized that MTZ bound to the β2 subunit of BHb, which further led to some changes of the skeleton and secondary structure of BHb. This research provides valuable information about the molecular mechanisms on BHb induced by MTZ and is beneficial for clarifying the toxicological actions of MTZ in blood.

Indexed as

Protein BindingAnimalsAntifungal AgentsBinding SitesCattleCircular DichroismEnvironmental PollutantsHemoglobinsHydrogen BondingMolecular Docking SimulationProtein SubunitsSerum Albumin, BovineSpectrometry, FluorescenceSpectrophotometry, UltravioletSpectrum AnalysisThermodynamics2-mercaptothiazolineAntifungal AgentsEnvironmental PollutantsHemoglobinsProtein SubunitsSerum Albumin, BovineThiazolidines2-MercaptothioazolineBinding interactionConformation investigationHemoglobinMolecular modelingSpectroscopic studies

Identifiers

PMID30387064
OpenAlexW2899509702

What OpenQuestion holds

Textmetadata
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.