Evidence map›Paper›PMID 34576913›Full record

ArticleMolecules (Basel, Switzerland)2021

Uptake of Cell-Penetrating Peptide RL2 by Human Lung Cancer Cells: Monitoring by Electron Paramagnetic Resonance and Confocal Laser Scanning Microscopy.

Sergey S Ovcherenko, Olga A Chinak, Anton V Chechushkov, Sergey A Dobrynin, Igor A Kirilyuk, Olesya A Krumkacheva, Vladimir A Richter, Elena G Bagryanskaya

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. 3,4-Unsubstituted 2-Molecules (Basel, Switzerland) · 2022
    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.

Sergey S OvcherenkoN.N. Vorozhtsov Novosibirsk Institute of Organic Chemistry SB RAS, 630090 Novosibirsk, Russia.
Olga A ChinakInstitute of Chemical Biology and Fundamental Medicine SB RAS, 630090 Novosibirsk, Russia.
Anton V ChechushkovInstitute of Chemical Biology and Fundamental Medicine SB RAS, 630090 Novosibirsk, Russia.
Sergey A DobryninN.N. Vorozhtsov Novosibirsk Institute of Organic Chemistry SB RAS, 630090 Novosibirsk, Russia.
Igor A KirilyukN.N. Vorozhtsov Novosibirsk Institute of Organic Chemistry SB RAS, 630090 Novosibirsk, Russia.ORCID 0000-0001-6033-0368
Olesya A KrumkachevaInternational Tomography Center SB RAS, 630090 Novosibirsk, Russia.ORCID 0000-0002-0777-5103
Vladimir A RichterInstitute of Chemical Biology and Fundamental Medicine SB RAS, 630090 Novosibirsk, Russia.
Elena G BagryanskayaN.N. Vorozhtsov Novosibirsk Institute of Organic Chemistry SB RAS, 630090 Novosibirsk, Russia.ORCID 0000-0003-0057-383X

Funding

Ministry of Science and Higher Education of the Russian Federation 14.W03.31.0034
6 · The paper itself

Abstract

RL2 is a recombinant analogue of a human κ-casein fragment, capable of penetrating cells and inducing apoptosis of cancer cells with no toxicity to normal cells. The exact mechanism of RL2 penetration into cells remains unknown. In this study, we investigated the mechanism of RL2 penetration into human lung cancer A549 cells by a combination of electron paramagnetic resonance (EPR) spectroscopy and confocal laser scanning microscopy. EPR spectra of A549 cells incubated with RL2 (sRL2) spin-labeled by a highly stable 3-carboxy-2,2,5,5-tetraethylpyrrolidine-1-oxyl radical were found to contain three components, with their contributions changing with time. The combined EPR and confocal-microscopy data allowed us to assign these three forms of sRL2 to the spin-labeled protein sticking to the membrane of the cell and endosomes, to the spin-labeled protein in the cell interior, and to spin labeled short peptides formed in the cell because of protein digestion. EPR spectroscopy enabled us to follow the kinetics of transformations between different forms of the spin-labeled protein at a minimal spin concentration (3-16 μM) in the cell. The prospects of applications of spin-labeled cell-penetrating peptides to EPR imaging, DNP, and magnetic resonance imaging are discussed, as is possible research on an intrinsically disordered protein in the cell by pulsed dipolar EPR spectroscopy.

Indexed as

Cell-Penetrating PeptidesLung NeoplasmsMicroscopy, ConfocalA549 CellsCell Line, TumorElectron Spin Resonance SpectroscopyHumansSpin LabelsCell-Penetrating PeptidesSpin Labelscell penetrating peptideconfocal microscopyelectron spin resonance spectroscopy

Identifiers

PMID34576913
PMCPMC8470091

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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.