Evidence map›Paper›PMID 34445319›Full record

ArticleInternational journal of molecular sciences2021

Membrane Association Modes of Natural Anticancer Peptides: Mechanistic Details on Helicity, Orientation, and Surface Coverage.

Mayra Quemé-Peña, Tünde Juhász, Gergely Kohut, Maria Ricci, Priyanka Singh, Imola Cs Szigyártó, Zita I Papp, Lívia Fülöp, Tamás Beke-Somfai

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. 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
2.0field-weighted citation impact, top 14% 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, 24 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

9 authors at 3 institutions in 1 country.

Mayra Quemé-PeñaBiomolecular Self-Assembly Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, H-1117 Budapest, Hungary.ORCID 0000-0002-0257-6594
Tünde JuhászBiomolecular Self-Assembly Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, H-1117 Budapest, Hungary.
Gergely KohutBiomolecular Self-Assembly Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, H-1117 Budapest, Hungary.ORCID 0000-0002-6139-5136
Maria RicciBiomolecular Self-Assembly Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, H-1117 Budapest, Hungary.
Priyanka SinghBiomolecular Self-Assembly Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, H-1117 Budapest, Hungary.
Imola Cs SzigyártóBiomolecular Self-Assembly Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, H-1117 Budapest, Hungary.ORCID 0000-0002-8551-8014
Zita I PappDepartment of Medical Chemistry, University of Szeged, Dóm tér 8, H-6720 Szeged, Hungary.ORCID 0000-0001-9202-9035
Lívia FülöpDepartment of Medical Chemistry, University of Szeged, Dóm tér 8, H-6720 Szeged, Hungary.ORCID 0000-0002-8010-0129
Tamás Beke-SomfaiBiomolecular Self-Assembly Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, H-1117 Budapest, Hungary.
Institute of Materials and Environmental Chemistry · HUEötvös Loránd University · HUUniversity of Szeged · HU

Funding

BIONANO_GINOP 2.3.2-15-2016-00017Hungarian Momentum Program LP2016-2National Competitiveness and Excellence Program NVKP_16-1-2016-0007
6 · The paper itself

Abstract

Anticancer peptides (ACPs) could potentially offer many advantages over other cancer therapies. ACPs often target cell membranes, where their surface mechanism is coupled to a conformational change into helical structures. However, details on their binding are still unclear, which would be crucial to reach progress in connecting structural aspects to ACP action and to therapeutic developments. Here we investigated natural helical ACPs, Lasioglossin LL-III, Macropin 1, Temporin-La, FK-16, and LL-37, on model liposomes, and also on extracellular vesicles (EVs), with an outer leaflet composition similar to cancer cells. The combined simulations and experiments identified three distinct binding modes to the membranes. Firstly, a highly helical structure, lying mainly on the membrane surface; secondly, a similar, yet only partially helical structure with disordered regions; and thirdly, a helical monomeric form with a non-inserted perpendicular orientation relative to the membrane surface. The latter allows large swings of the helix while the N-terminal is anchored to the headgroup region. These results indicate that subtle differences in sequence and charge can result in altered binding modes. The first two modes could be part of the well-known carpet model mechanism, whereas the newly identified third mode could be an intermediate state, existing prior to membrane insertion.

Indexed as

Amino Acid MotifsAntimicrobial Cationic PeptidesAntineoplastic AgentsBee VenomsCathelicidinsCell MembraneExtracellular VesiclesHumansProtein BindingProtein DomainsAntimicrobial Cationic PeptidesAntineoplastic AgentsBee VenomsCathelicidinsmacropin, Macropis fulvipestemporinanticancer peptidesflow-linear dichroismmolecular dynamicspeptide conformationspectroscopy

Identifiers

PMID34445319
PMCPMC8395313
OpenAlexW3188618095

What OpenQuestion holds

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LicenceCC BY
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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.