Evidence map›Paper›PMID 32363265›Full record

ArticleACS omega2020

Spectroscopic and Molecular Docking Investigation on the Noncovalent Interaction of Lysozyme with Saffron Constituent "Safranal".

Mohd Sajid Ali, Hamad A Al-Lohedan

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

10 citing papers in PubMed, 73 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.

Mohd Sajid AliSurfactant Research Chair, Department of Chemistry, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi Arabia.
Hamad A Al-LohedanSurfactant Research Chair, Department of Chemistry, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi Arabia.
King Saud University · SA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Owing to the various beneficial properties of the popular spice saffron, the interaction of safranal, a secondary metabolite of the former, with hen egg white lysozyme was investigated. The formation of a complex was evidenced by UV-visible spectroscopy. Fluorescence quenching experiments were also performed to understand the binding mechanism and to evaluate the forces involved in binding. The strong absorption of safranal in the range of excitation and emission wavelengths of lysozyme fluorescence required the correction of the inner filter effect for fluorescence spectra to obtain the apparent extent of binding. There was a considerable difference between the observed spectra and corrected spectra, and a similar observation was found in the case of synchronous fluorescence spectra. From the analysis of quenching data, it was found that the mechanism involved in quenching was static with 1:1 binding between them. The interaction was found to be driven, mainly, by hydrophobic forces and hydrogen bonding. Safranal had negligible impact on the secondary structure of lysozyme. The interaction was also studied by molecular docking, and the results were in good agreement with the results obtained experimentally. The binding site of safranal was in the big hydrophobic cavity of lysozyme. The amino acids involved in the interaction were Asp52, Ile58, Gln57, Asn59, Trp62, Trp63, Trp108, Ile98, Asp101, and Ala107.

Identifiers

PMID32363265
PMCPMC7191604
OpenAlexW3016272514

What OpenQuestion holds

Textmetadata
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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.