Evidence map›Paper›PMID 24319355›Full record

ArticleTheScientificWorldJournal2013

Studies of the interaction between isoimperatorin and human serum albumin by multispectroscopic method: identification of possible binding site of the compound using esterase activity of the protein.

Samira Ranjbar, Yalda Shokoohinia, Sirous Ghobadi, Nooshin Bijari, Saeed Gholamzadeh, Nastaran Moradi, Mohammad Reza Ashrafi-Kooshk, Abbas Aghaei, Reza Khodarahmi

Open access · goldAbstract read
In one paragraph

Article in TheScientificWorldJournal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-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

17 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Food Antioxidants and Their Interaction with Human Proteins.Antioxidants (Basel, Switzerland) · 2023
    Review
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  6. Acridine BasedMolecules (Basel, Switzerland) · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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 3 institutions in 1 country.

Samira RanjbarNano Drug Delivery Research Center, Kermanshah University of Medical Sciences, Kermanshah 6734667149, Iran.
Yalda Shokoohinia
Sirous Ghobadi
Nooshin Bijari
Saeed Gholamzadeh
Nastaran Moradi
Mohammad Reza Ashrafi-Kooshk
Abbas Aghaei
Reza Khodarahmi
Kermanshah University of Medical Sciences · IRIsfahan University of Medical Sciences · IRRazi University · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Isoimperatorin is one of the main components of Prangos ferulacea as a linear furanocoumarin and used as anti-inflammatory, analgesic, antispasmodic, and anticancer drug. Human serum albumin (HSA) is a principal extracellular protein with a high concentration in blood plasma and carrier for many drugs to different molecular targets. Since the carrying of drug by HSA may affect on its structure and action, we decided to investigate the interaction between HSA and isoimperatorin using fluorescence and UV spectroscopy. Fluorescence data indicated that isoimperatorin quenches the intrinsic fluorescence of the HSA via a static mechanism and hydrophobic interaction play the major role in the drug binding. The binding average distance between isoimperatorin and Trp 214 of HSA was estimated on the basis of the theory of Förster energy transfer. Decrease of protein surface hydrophobicity (PSH) was also documented upon isoimperatorin binding. Furthermore, the synchronous fluorescence spectra show that the microenvironment of the tryptophan residues does not have obvious changes. Site marker compettive and fluorescence experiments revealed that the binding of isoimperatorin to HSA occurred at or near site I. Finally, the binding details between isoimperatorin and HSA were further confirmed by molecular docking and esterase activity inhibition studies which revealed that drug was bound at subdomain IIA.

Indexed as

Molecular Docking SimulationBinding SitesEsterasesHumansHydrophobic and Hydrophilic InteractionsProtein BindingProtein Structure, TertiarySerum AlbuminSpectrophotometry, UltravioletTryptophanEsterasesSerum AlbuminTryptophan

Identifiers

PMID24319355
PMCPMC3844181
OpenAlexW1974630059

What OpenQuestion holds

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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.