Evidence map›Paper›PMID 35457032›Full record

ArticleInternational journal of molecular sciences2022

Conformational Changes in the BSA-LT4 Complex Induced by the Presence of Vitamins: Spectroscopic Approach and Molecular Docking.

Nicoleta Cazacu, Claudia G Chilom, Melinda David, Monica Florescu

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 42% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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

4 authors at 2 institutions in 1 country.

Nicoleta CazacuDepartment of Electricity, Solid Physics and Biophysics, Faculty of Physics, University of Bucharest, Str. Atomistilor No. 405, CP MG-11, Bucuresti-Magurele, 077125 Magurele, Romania.
Claudia G ChilomDepartment of Electricity, Solid Physics and Biophysics, Faculty of Physics, University of Bucharest, Str. Atomistilor No. 405, CP MG-11, Bucuresti-Magurele, 077125 Magurele, Romania.ORCID 0000-0003-3662-9268
Melinda DavidDepartment of Fundamental, Prophylactic and Clinical Disciplines, Faculty of Medicine, Transilvania University of Brasov, Str. Universitatii No. 1, Building C, Room CI30, 500068 Brasov, Romania.ORCID 0000-0002-2971-4547
Monica FlorescuDepartment of Fundamental, Prophylactic and Clinical Disciplines, Faculty of Medicine, Transilvania University of Brasov, Str. Universitatii No. 1, Building C, Room CI30, 500068 Brasov, Romania.ORCID 0000-0002-1467-3113
Transylvania University of Brașov · ROUniversity of Bucharest · RO

Funding

Ministerul Cercetării și Inovării project number PN-III-P1-1.2-PCCDI-2017-0062, contract no. 58, within PNCDI III
6 · The paper itself

Abstract

Levothyroxine (LT4) is known for its use in various conditions including hypothyroidism. LT4 interaction with serum albumin may be influenced by the presence of vitamins. For this reason, we investigated the effect of vitamin C, vitamin B12, and folic acid on the complex of Bovine Serum Albumin with LT4 (BSA-LT4). UV-Vis spectroscopy was used to monitor the influence of vitamins on the BSA-LT4 complex. Fluorescence spectroscopy revealed a static quenching mechanism of the fluorescence of BSA-LT4 complex by the vitamin C and folic acid and a combined mechanism for vitamin B12. The interaction of vitamin C and folic acid with BSA-LT4 was moderate, while the binding of vitamin B12 was much stronger, extending the storage time of LT4 in blood plasma. Synchronous fluorescence found that the vitamins were closer to the vicinity of Trp than to Tyr and the effect was more pronounced for the binding of vitamin B12. The thermal stability of the BSA-LT4 complex was more evident, but no influence on the stability of BSA-LT4 complex was obtained for vitamin C. Molecular docking studies showed that vitamin C and folic acid bound the same site of the protein, while vitamin B12 bonded to a different site.

Indexed as

Serum Albumin, BovineVitaminsAscorbic AcidBinding SitesFolic AcidMolecular Docking SimulationProtein BindingSpectrometry, FluorescenceSpectrophotometry, UltravioletThermodynamicsThyroxineVitamin AVitamin B 12Vitamin KAscorbic AcidFolic AcidSerum Albumin, BovineThyroxineVitamin AVitamin B 12Vitamin KVitaminsBSA-LT4 complexmolecular dockingspectroscopyvitamins

Identifiers

PMID35457032
PMCPMC9027512
OpenAlexW4223454552

What OpenQuestion holds

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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.