Evidence map›Paper›PMID 36083171›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2022

Ionic Strength and Solution Composition Dictate the Adsorption of Cell-Penetrating Peptides onto Phosphatidylcholine Membranes.

Man Thi Hong Nguyen, Denys Biriukov, Carmelo Tempra, Katarina Baxova, Hector Martinez-Seara, Hüseyin Evci, Vandana Singh, Radek Šachl, Martin Hof, Pavel Jungwirth and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2022. 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
2.3field-weighted citation impact, top 11% 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

13 citing papers in PubMed, 30 citations in OpenAlex.

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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

12 authors at 5 institutions in 2 countries.

Man Thi Hong NguyenInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 542/2, CZ-16000 Prague 6, Czech Republic.ORCID 0000-0002-9700-3333
Denys BiriukovInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 542/2, CZ-16000 Prague 6, Czech Republic.ORCID 0000-0003-1007-2203
Carmelo TempraInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 542/2, CZ-16000 Prague 6, Czech Republic.ORCID 0000-0002-2890-6993
Katarina BaxovaInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 542/2, CZ-16000 Prague 6, Czech Republic.
Hector Martinez-SearaInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 542/2, CZ-16000 Prague 6, Czech Republic.ORCID 0000-0001-9716-1713
Hüseyin EvciJ. Heyrovský Institute of Physical Chemistry of the Czech Academy of Sciences, Dolejškova 2155/3, CZ-18223 Prague 8, Czech Republic.
Vandana SinghJ. Heyrovský Institute of Physical Chemistry of the Czech Academy of Sciences, Dolejškova 2155/3, CZ-18223 Prague 8, Czech Republic.
Radek ŠachlJ. Heyrovský Institute of Physical Chemistry of the Czech Academy of Sciences, Dolejškova 2155/3, CZ-18223 Prague 8, Czech Republic.ORCID 0000-0002-0441-3908
Martin HofJ. Heyrovský Institute of Physical Chemistry of the Czech Academy of Sciences, Dolejškova 2155/3, CZ-18223 Prague 8, Czech Republic.
Pavel JungwirthInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 542/2, CZ-16000 Prague 6, Czech Republic.ORCID 0000-0002-6892-3288
Matti JavanainenInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 542/2, CZ-16000 Prague 6, Czech Republic.ORCID 0000-0003-4858-364X
Mario VazdarInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo nám. 542/2, CZ-16000 Prague 6, Czech Republic.ORCID 0000-0001-6905-6174
Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZCzech Academy of Sciences, J. Heyrovský Institute of Physical Chemistry · CZCharles University · CZUniversity of Helsinki · FIUniversity of South Bohemia in České Budějovice · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adsorption of arginine-rich positively charged peptides onto neutral zwitterionic phosphocholine (PC) bilayers is a key step in the translocation of those potent cell-penetrating peptides into the cell interior. In the past, we have shown both theoretically and experimentally that polyarginines adsorb to the neutral PC-supported lipid bilayers in contrast to polylysines. However, comparing our results with previous studies showed that the results often do not match even at the qualitative level. The adsorption of arginine-rich peptides onto 1-palmitoyl-2-oleoyl-

Indexed as

Cell-Penetrating PeptidesLipid BilayersAdsorptionArginineLecithinsOsmolar ConcentrationPhosphatidylcholinesPhosphorylcholineArginineCell-Penetrating PeptidesLecithinsLipid BilayersPhosphatidylcholinesPhosphorylcholine

Identifiers

PMID36083171
PMCPMC9494944
OpenAlexW4295038050

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.