Evidence map›Paper›PMID 29679078›Full record

ArticleScientific reports2018

Fluorophore labeling of a cell-penetrating peptide significantly alters the mode and degree of biomembrane interaction.

Sofie Fogh Hedegaard, Mohammed Sobhi Derbas, Tania Kjellerup Lind, Marina Robertnova Kasimova, Malene Vinther Christensen, Maria Høtoft Michaelsen, Richard A Campbell, Lene Jorgensen, Henrik Franzyk, Marité Cárdenas and 1 more

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 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

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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

11 authors.

Sofie Fogh HedegaardDepartment of Pharmacy, Faculty of Health and Medical Sciences, University of Copenhagen, Universitetsparken 2, 2100, Copenhagen, Denmark.
Mohammed Sobhi DerbasDepartment of Pharmacy, Faculty of Health and Medical Sciences, University of Copenhagen, Universitetsparken 2, 2100, Copenhagen, Denmark.
Tania Kjellerup LindDepartment of Biomedical Science and Biofilms - Research Center for Biointerfaces, Faculty of Health and Society, Malmö University, Per Albin Hanssons väg 35, 214 32, Malmö, Sweden.
Marina Robertnova KasimovaDepartment of Pharmacy, Faculty of Health and Medical Sciences, University of Copenhagen, Universitetsparken 2, 2100, Copenhagen, Denmark.
Malene Vinther ChristensenDepartment of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Jagtvej 162, 2100, Copenhagen, Denmark.
Maria Høtoft MichaelsenDepartment of Pharmacy, Faculty of Health and Medical Sciences, University of Copenhagen, Universitetsparken 2, 2100, Copenhagen, Denmark.
Richard A CampbellInstitut Laue-Langevin, 71 avenue des Martyrs, CS20156, 38042, Grenoble, France.
Lene JorgensenDepartment of Pharmacy, Faculty of Health and Medical Sciences, University of Copenhagen, Universitetsparken 2, 2100, Copenhagen, Denmark.
Henrik FranzykDepartment of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Jagtvej 162, 2100, Copenhagen, Denmark.
Marité CárdenasDepartment of Biomedical Science and Biofilms - Research Center for Biointerfaces, Faculty of Health and Society, Malmö University, Per Albin Hanssons väg 35, 214 32, Malmö, Sweden. marite.cardenas@mah.se.ORCID 0000-0003-0392-3540
Hanne Mørck NielsenDepartment of Pharmacy, Faculty of Health and Medical Sciences, University of Copenhagen, Universitetsparken 2, 2100, Copenhagen, Denmark. hanne.morck@sund.ku.dk.ORCID 0000-0002-7285-9100

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The demand for highly efficient macromolecular drugs, used in the treatment of many severe diseases, is continuously increasing. However, the hydrophilic character and large molecular size of these drugs significantly limit their ability to permeate across cellular membranes and thus impede the drugs in reaching their target sites in the body. Cell-penetrating peptides (CPP) have gained attention as promising drug excipients, since they can facilitate drug permeation across cell membranes constituting a major biological barrier. Fluorophores are frequently covalently conjugated to CPPs to improve detection, however, the ensuing change in physico-chemical properties of the CPPs may alter their biological properties. With complementary biophysical techniques, we show that the mode of biomembrane interaction may change considerably upon labeling of the CPP penetratin (PEN) with a fluorophore. Fluorophore-PEN conjugates display altered modes of membrane interaction with increased insertion into the core of model cell membranes thereby exerting membrane-thinning effects. This is in contrast to PEN, which localizes along the head groups of the lipid bilayer, without affecting the thickness of the lipid tails. Particularly high membrane disturbance is observed for the two most hydrophobic PEN conjugates; rhodamine B or 1-pyrene butyric acid, as compared to the four other tested fluorophore-PEN conjugates.

Indexed as

Amino Acid SequenceCarrier ProteinsCell MembraneCell Membrane PermeabilityCell-Penetrating PeptidesFluorescent DyesHydrophobic and Hydrophilic InteractionsIonophoresLipid BilayersRhodaminesCarrier ProteinsCell-Penetrating PeptidesFluorescent DyesIonophoresLipid Bilayerspenetratinrhodamine BRhodamines

Identifiers

PMID29679078
PMCPMC5910404

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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.