Evidence map›Paper›PMID 27959940›Full record

ArticlePloS one2016

Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study.

Milica Radibratovic, Simeon Minic, Dragana Stanic-Vucinic, Milan Nikolic, Milos Milcic, Tanja Cirkovic Velickovic

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 43 citations in OpenAlex.

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  6. Food Antioxidants and Their Interaction with Human Proteins.Antioxidants (Basel, Switzerland) · 2023
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  14. C-phycoerythrin fromMarine drugs · 2021
    Article
  15. Article
  16. 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

6 authors at 3 institutions in 3 countries.

Milica RadibratovicInstitute of Chemistry, Technology and Metallurgy - Center for Chemistry, University of Belgrade, Belgrade, Serbia.
Simeon MinicCenter of Excellence for Molecular Food Sciences, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia.
Dragana Stanic-VucinicCenter of Excellence for Molecular Food Sciences, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia.
Milan NikolicCenter of Excellence for Molecular Food Sciences, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia.
Milos MilcicDepartment of Inorganic Chemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia.
Tanja Cirkovic VelickovicCenter of Excellence for Molecular Food Sciences, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia.
University of Belgrade · RSUniversity of Belgrade – Faculty of ChemistryGhent University Global Campus · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phycocyanobilin (PCB) binds with high affinity (2.2 x 106 M-1 at 25°C) to human serum albumin (HSA) at sites located in IB and IIA subdomains. The aim of this study was to examine effects of PCB binding on protein conformation and stability. Using 300 ns molecular dynamics (MD) simulations, UV-VIS spectrophotometry, CD, FT-IR, spectrofluorimetry, thermal denaturation and susceptibility to trypsin digestion, we studied the effects of PCB binding on the stability and rigidity of HSA, as well as the conformational changes in PCB itself upon binding to the protein. MD simulation results demonstrated that HSA with PCB bound at any of the two sites showed greater rigidity and lower overall and individual domain flexibility compared to free HSA. Experimental data demonstrated an increase in the α-helical content of the protein and thermal and proteolytic stability upon ligand binding. PCB bound to HSA undergoes a conformational change to a more elongated conformation in the binding pockets of HSA. PCB binding to HSA stabilizes the structure of this flexible transport protein, making it more thermostable and resistant to proteolysis. The results from this work explain at molecular level, conformational changes and stabilization of HSA structure upon ligand binding. The resultant increased thermal and proteolytic stability of HSA may provide greater longevity to HSA in plasma.

Indexed as

Molecular Docking SimulationBinding SitesPhycobilinsPhycocyaninProtein BindingProtein StabilitySerum AlbuminSpirulinaPhycobilinsPhycocyaninphycocyanobilinSerum Albumin

Identifiers

PMID27959940
PMCPMC5154526
OpenAlexW2561605235

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.