Evidence map›Paper›PMID 34443680›Full record

ArticleMolecules (Basel, Switzerland)2021

Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods.

Ruichen Zhao, Xiaoli Qin, Jinfeng Zhong

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

7 citing papers in PubMed, 23 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Ruichen ZhaoCollege of Food Science, Southwest University, Chongqing 400715, China.ORCID 0000-0002-9102-8628
Xiaoli QinCollege of Food Science, Southwest University, Chongqing 400715, China.ORCID 0000-0001-6404-4836
Jinfeng ZhongCollege of Food Science, Southwest University, Chongqing 400715, China.
Southwest University · CN

Funding

Chongqing Municipal Training Program of Innovation and Entrepreneurship for Undergraduates S202010635165Fundamental Research Funds for the Central Universities XDJK2019B056Venture & Innovation Support Program for Chongqing Overseas Returnees cx2018098
6 · The paper itself

Abstract

Effect of temperature and pH on the interaction of curcumin with β-casein was explored by fluorescence spectroscopy, ultraviolet-visible spectroscopy and molecular dynamics simulation. The spectroscopic results showed that curcumin could bind to β-casein to form a complex which was driven mainly by electrostatic interaction. The intrinsic fluorescence of β-casein was quenched by curcumin through static quenching mechanism. The binding constants of curcumin to β-casein were 6.48 × 10

Indexed as

Molecular Dynamics SimulationSpectrum AnalysisCaseinsCurcuminHydrogen BondingHydrogen-Ion ConcentrationImaging, Three-DimensionalMolecular Docking SimulationProtein BindingProtein Structure, SecondaryStructural Homology, ProteinThermodynamicsCaseinsCurcuminfluorescence quenchinghydrophobic interactionmolecular dockingsecondary structure contentthermodynamic parameters

Identifiers

PMID34443680
PMCPMC8398086
OpenAlexW3193289065

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.