Evidence map›Paper›PMID 31153187›Full record

ArticleThe Journal of chemical physics2019

Exploring the impact of proteins on the line tension of a phase-separating ternary lipid mixture.

Asanga Bandara, Afra Panahi, George A Pantelopulos, Tetsuro Nagai, John E Straub

Open access · greenAbstract read
In one paragraph

Article in The Journal of chemical physics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

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  12. Interleaflet Coupling of Lipid Nanodomains - Insights FromFrontiers in cell and developmental biology · 2020
    Review
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

5 authors at 2 institutions in 2 countries.

Asanga BandaraDepartment of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, Massachusetts 02215, USA.ORCID 0000000312647330
Afra PanahiDepartment of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, Massachusetts 02215, USA.
George A PantelopulosDepartment of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, Massachusetts 02215, USA.ORCID 0000000243731677
Tetsuro NagaiDepartment of Physics, Graduate School of Science, Nagoya University, Nagoya, Aichi 464-8602, Japan.ORCID 0000000286854220
John E StraubDepartment of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, Massachusetts 02215, USA.ORCID 0000000223553316
Boston University · USNagoya University · JP

Funding

Probing the roles of membrane and cholesterol on Aβ biogenesis and prion protein interactionsR01GM107703 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI STRAUB, JOHN E., THIRUMALAI, DEVARAJAN · 2015 to 2022
$2.7M
NIGMS NIH HHS R01 GM107703
6 · The paper itself

Abstract

The separation of lipid mixtures into thermodynamically stable phase-separated domains is dependent on lipid composition, temperature, and system size. Using molecular dynamics simulations, the line tension between thermodynamically stable lipid domains formed from ternary mixtures of di-C16:0 PC:di-C18:2 PC:cholesterol at 40:40:20 mol. % ratio was investigated via two theoretical approaches. The line tension was found to be 3.1 ± 0.2 pN by capillary wave theory and 4.7 ± 3.7 pN by pressure tensor anisotropy approaches for coarse-grained models based on the Martini force field. Using an all-atom model of the lipid membrane based on the CHARMM36 force field, the line tension was found to be 3.6 ± 0.9 pN using capillary wave theory and 1.8 ± 2.2 pN using pressure anisotropy approaches. The discrepancy between estimates of the line tension based on capillary wave theory and pressure tensor anisotropy methods is discussed. Inclusion of protein in Martini membrane lipid mixtures was found to reduce the line tension by 25%-35% as calculated by the capillary wave theory approach. To further understand and predict the behavior of proteins in phase-separated membranes, we have formulated an analytical Flory-Huggins model and parameterized it against the simulation results. Taken together these results suggest a general role for proteins in reducing the thermodynamic cost associated with domain formation in lipid mixtures and quantifies the thermodynamic driving force promoting the association of proteins to domain interfaces.

Identifiers

PMID31153187
PMCPMC6879351
OpenAlexW2945836084

What Socratic holds

Textmetadata
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 Socratic graph.