Evidence map›Paper›PMID 26331251›Full record

ArticleBiophysical journal2015

PE and PS Lipids Synergistically Enhance Membrane Poration by a Peptide with Anticancer Properties.

Natália Bueno Leite, Anders Aufderhorst-Roberts, Mario Sergio Palma, Simon D Connell, João Ruggiero Neto, Paul A Beales

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2015. 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
5.0field-weighted citation impact, top 4% 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

50 citing papers in PubMed, 122 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

6 authors at 3 institutions in 2 countries.

Natália Bueno LeiteDepartment of Physics, Instituto de Biociências Letras e Ciências Exatas, São Paulo State University, Universidade Estadual Paulista "Júlio de Mesquita Filho", São Paulo, Brazil.
Anders Aufderhorst-RobertsSchool of Physics and Astronomy and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK.
Mario Sergio PalmaCenter of Studies of Social Insects and Department of Biology and Instituto de Biociências, São Paulo State University, Universidade Estadual Paulista "Júlio de Mesquita Filho", São Paulo, Brazil.
Simon D ConnellSchool of Physics and Astronomy and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK.
João Ruggiero NetoDepartment of Physics, Instituto de Biociências Letras e Ciências Exatas, São Paulo State University, Universidade Estadual Paulista "Júlio de Mesquita Filho", São Paulo, Brazil. Electronic address: jruggiero@sjrp.unesp.br.
Paul A BealesSchool of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK. Electronic address: p.a.beales@leeds.ac.uk.
Universidade Estadual Paulista (Unesp) · BRInstitute of Structural and Molecular Biology · GBUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polybia-MP1 (MP1) is a bioactive host-defense peptide with known anticancer properties. Its activity is attributed to excess serine (phosphatidylserine (PS)) on the outer leaflet of cancer cells. Recently, higher quantities of phosphatidylethanolamine (PE) were also found at these cells' surface. We investigate the interaction of MP1 with model membranes in the presence and absence of POPS (PS) and DOPE (PE) to understand the role of lipid composition in MP1's anticancer characteristics. Indeed we find that PS lipids significantly enhance the bound concentration of peptide on the membrane by a factor of 7-8. However, through a combination of membrane permeability assays and imaging techniques we find that PE significantly increases the susceptibility of the membrane to disruption by these peptides and causes an order-of-magnitude increase in membrane permeability by facilitating the formation of larger transmembrane pores. Significantly, atomic-force microscopy imaging reveals differences in the pore formation mechanism with and without the presence of PE. Therefore, PS and PE lipids synergistically combine to enhance membrane poration by MP1, implying that the combined enrichment of both these lipids in the outer leaflet of cancer cells is highly significant for MP1's anticancer action. These mechanistic insights could aid development of novel chemotherapeutics that target pathological changes in the lipid composition of cancerous cells.

Indexed as

Antimicrobial Cationic PeptidesAntineoplastic AgentsCell MembraneCell Membrane PermeabilityDose-Response Relationship, DrugKineticsPhosphatidylethanolaminesPhosphatidylserinesPorosityUnilamellar LiposomesWasp VenomsAntimicrobial Cationic PeptidesAntineoplastic AgentsphosphatidylethanolaminePhosphatidylethanolaminesPhosphatidylserinespolybia-MPI, Polybia paulistaUnilamellar LiposomesWasp Venoms

Identifiers

PMID26331251
PMCPMC4564682
OpenAlexW1911688337

What OpenQuestion holds

Textmetadata
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.