Evidence map›Paper›PMID 29588488›Full record

ArticleScientific reports2018

Dynamic analysis of the interactions between Si/SiO

Miruna Silvia Stan, Ludmila Otilia Cinteza, Livia Petrescu, Maria Alexandra Mernea, Octavian Calborean, Dan Florin Mihailescu, Cornelia Sima, Anca Dinischiotu

Abstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Tracing theEnvironment & health (Washington, D.C.) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Influence of Proteins on Bioaccessibility ofFoods (Basel, Switzerland) · 2023
    Article
  8. Review
  9. Article
  10. Review
  11. Analysing the nanoparticle-protein corona for potential molecular target identification.Journal of controlled release : official journal of the Controlled Release Society · 2020
    Review
  12. Article
  13. 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

8 authors.

Miruna Silvia StanUniversity of Bucharest, Faculty of Biology, Department of Biochemistry and Molecular Biology, 91-95 Splaiul Independentei, 050095, Bucharest, Romania.
Ludmila Otilia CintezaUniversity of Bucharest, Faculty of Chemistry, 4-12 Bd. Regina Elisabeta, 030018, Bucharest, Romania. ocinteza@yahoo.com.
Livia PetrescuUniversity of Bucharest, Faculty of Biology, Department of Anatomy, Animal Physiology and Biophysics, 91-95 Splaiul Independentei, 050095, Bucharest, Romania.
Maria Alexandra MerneaUniversity of Bucharest, Faculty of Biology, Department of Anatomy, Animal Physiology and Biophysics, 91-95 Splaiul Independentei, 050095, Bucharest, Romania.
Octavian CalboreanUniversity of Bucharest, Faculty of Biology, Department of Anatomy, Animal Physiology and Biophysics, 91-95 Splaiul Independentei, 050095, Bucharest, Romania.
Dan Florin MihailescuUniversity of Bucharest, Faculty of Biology, Department of Anatomy, Animal Physiology and Biophysics, 91-95 Splaiul Independentei, 050095, Bucharest, Romania.
Cornelia SimaNational Institute for Laser, Plasma and Radiation Physics, 409 Atomistilor, 077125, Bucharest-Magurele, Romania.
Anca DinischiotuUniversity of Bucharest, Faculty of Biology, Department of Biochemistry and Molecular Biology, 91-95 Splaiul Independentei, 050095, Bucharest, Romania. anca.dinischiotu@bio.unibuc.ro.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Due to their outstanding properties, quantum dots (QDs) received a growing interest in the biomedical field, but it is of major importance to investigate and to understand their interaction with the biomolecules. We examined the stability of silicon QDs and the time evolution of QDs - protein corona formation in various biological media (bovine serum albumin, cell culture medium without or supplemented with 10% fetal bovine serum-FBS). Changes in the secondary structure of BSA were also investigated over time. Hydrodynamic size and zeta potential measurements showed an evolution in time indicating the nanoparticle-protein interaction. The protein corona formation was also dependent on time, albumin adsorption reaching the peak level after 1 hour. The silicon QDs adsorbed an important amount of FBS proteins from the first 5 minutes of incubation that was maintained for the next 8 hours, and diminished afterwards. Under protein-free conditions the QDs induced cell membrane damage in a time-dependent manner, however the presence of serum proteins attenuated their hemolytic activity and maintained the integrity of phosphatidylcholine layer. This study provides useful insights regarding the dynamics of BSA adsorption and interaction of silicon QDs with proteins and lipids, in order to understand the role of QDs biocorona.

Indexed as

AdsorptionAnimalsCattleHemolysisHumansProtein CoronaProtein Structure, SecondaryQuantum DotsSerum Albumin, BovineSiliconSilicon DioxideProtein CoronaSerum Albumin, BovineSiliconSilicon Dioxide

Identifiers

PMID29588488
PMCPMC5869727

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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.