Evidence map›Paper›PMID 27722919›Full record

ArticleJournal of fluorescence2017

Comparative Study of the Interactions between Ovalbumin and five Antioxidants by Spectroscopic Methods.

Xiangrong Li, Yunhui Yan

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Journal of fluorescence, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

4 citing papers in PubMed, 31 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

2 authors at 1 institution in 1 country.

Xiangrong LiDepartment of Chemistry, Key Laboratory of Medical Molecular Probes, School of Basic Medicine, Xinxiang Medical University, 601 Jin-sui Road, Hong Qi District, Xinxiang, 453003, People's Republic of China.
Yunhui YanDepartment of Chemistry, Key Laboratory of Medical Molecular Probes, School of Basic Medicine, Xinxiang Medical University, 601 Jin-sui Road, Hong Qi District, Xinxiang, 453003, People's Republic of China. 2645974654@qq.com.
Xinxiang Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-Ascorbic acid, α-tocopherol, procyanidin B3, β-carotene and astaxanthin are five classic dietary antioxidants. In this study, the interaction between the five antioxidants and ovalbumin was investigated by fluorescence spectroscopy, in combination with UV-vis absorption spectroscopy and circular dichroism (CD) spectroscopy. The quenching mechanism of ovalbumin by α-tocopherol is static quenching and the interaction between α-tocopherol and ovalbumin is synergistically driven by enthalpy and entropy. Electrostatic interactions and hydrophobic interactions play a major role in stabilizing the complex. For the other four antioxidants, the quenching mechanisms are all static quenching mechanisms at lower concentrations of antioxidants, but at higher concentrations of antioxidants, predominantly by the "sphere of action" quenching mechanisms. The binding processes of the other four antioxidants to ovalbumin are all entropy process and the major part of the action force is hydrophobic interactions. The binding constants of ovalbumin with the five antioxidants are in the following order as: astaxanthin > β-carotene > L-ascorbic acid > procyanidin B3 > α-tocopherol at 298 K. Synchronous fluorescence spectroscopy shows the interaction between L-ascorbic acid/β-carotene/astaxanthin and ovalbumin decreases the hydrophobicity of the microenvironment of tryptophan (Trp) and tyrosine (Tyr) residues. The hydrophobicity of Trp is increased while the hydrophility of Tyr is increased in the presence of α-tocopherol. However, the microenvironment of Trp and Tyr is not affected by procyanidin B3. The UV-vis absorption and CD spectra suggest that the interaction between the five antioxidants and ovalbumin leads to the loosening and unfolding of ovalbumin skeleton and exerts some influence on the natural secondary structure of ovalbumin. The study provides an accurate and full basic data for clarifying the binding mechanisms of L-ascorbic acid, α-tocopherol, procyanidin B3, β-carotene and astaxanthin interacting with ovalbumin and is helpful for understanding rational use of antioxidants as dietary supplements.

Indexed as

alpha-TocopherolAnimalsAntioxidantsAscorbic Acidbeta CaroteneBiflavonoidsBinding SitesCatechinCircular DichroismHumansOvalbuminProanthocyanidinsProtein BindingSpectrometry, FluorescenceThermodynamicsXanthophyllsalpha-TocopherolAntioxidantsAscorbic Acidastaxanthinebeta CaroteneBiflavonoidsCatechinOvalbuminProanthocyanidinsprocyanidin B3XanthophyllsAntioxidantsCircular dichroism spectroscopyFluorescence spectroscopyInteractionOvalbuminUV-vis absorption spectroscopy

Identifiers

PMID27722919
OpenAlexW2528340840

What OpenQuestion holds

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Registered trials

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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.