Evidence map›Paper›PMID 36985629›Full record

ArticleMolecules (Basel, Switzerland)2023

Characterization of the Interactions between Minocycline Hydrochloride and Trypsin with Spectroscopic and Molecular Docking Technology.

Xiaoxia Wang, Jisheng Sun, Litong Ma, Zhihua Nie, Huazheng Sai, Jianguo Cheng, Jianguo Duan

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecules (Basel, Switzerland), 2023. 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
1.8field-weighted citation impact, top 15% 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, 12 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

7 authors at 2 institutions in 1 country.

Xiaoxia WangSchool of Chemistry and Chemical Engineering, Inner Mongolia University of Science and Technology, Baotou 014010, China.
Jisheng SunSchool of Chemistry and Chemical Engineering, Inner Mongolia University of Science and Technology, Baotou 014010, China.
Litong MaSchool of Chemistry and Chemical Engineering, Inner Mongolia University of Science and Technology, Baotou 014010, China.ORCID 0000-0002-9850-2601
Zhihua NieSchool of Life Sciences, Tsinghua University, Beijing 100084, China.ORCID 0009-0009-9256-1828
Huazheng SaiSchool of Chemistry and Chemical Engineering, Inner Mongolia University of Science and Technology, Baotou 014010, China.
Jianguo ChengSchool of Chemistry and Chemical Engineering, Inner Mongolia University of Science and Technology, Baotou 014010, China.
Jianguo DuanSchool of Chemistry and Chemical Engineering, Inner Mongolia University of Science and Technology, Baotou 014010, China.
Inner Mongolia University of Science and Technology · CNTsinghua University · CN

Funding

School of Chemistry and Chemical Engineering, Inner Mongolia University of Science and Technology 014010
6 · The paper itself

Abstract

In the current study, the interaction of minocycline hydrochloride (MC) and trypsin (TRP) was studied using fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy, UV-Vis spectroscopy, and molecular docking simulation techniques. The results show that the fluorescence quenching of trypsin at different degrees can be caused by minocycline hydrochloride at different temperatures. According to the Stern-Volmer equation, the fluorescence quenching type was static quenching. By calculating critical distance, we concluded that there is a possibility of non-radiative energy transfer between minocycline hydrochloride and trypsin. The effect of minocycline hydrochloride on the secondary structure of trypsin was demonstrated using ultraviolet spectroscopy. Synchronous fluorescence spectroscopy showed that minocycline hydrochloride could bind to tryptophan residues in trypsin, resulting in corresponding changes in the secondary structure of trypsin. Three-dimensional fluorescence spectroscopy showed that minocycline hydrochloride had a particular effect on the microenvironment of trypsin that led to changes in the secondary structure of trypsin. The molecular docking technique demonstrated that the binding of minocycline hydrochloride and trypsin was stable. Circular dichroism showed that the secondary structure of trypsin could be changed by minocycline hydrochloride.

Indexed as

MinocyclineBinding SitesCircular DichroismMolecular Docking SimulationProtein BindingSpectrometry, FluorescenceSpectrophotometry, UltravioletThermodynamicsTrypsinMinocyclineTrypsinminocycline hydrochloridemolecular docking simulation methodmultispectral analysistrypsin

Identifiers

PMID36985629
PMCPMC10051561
OpenAlexW4324365725

What OpenQuestion holds

Textmetadata
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.