Evidence map›Paper›PMID 38815687›Full record

ArticleBiochimica et biophysica acta. Biomembranes2024

Neutron spin echo shows pHLIP is capable of retarding membrane thickness fluctuations.

Haden L Scott, Violeta Burns-Casamayor, Andrew C Dixson, Robert F Standaert, Christopher B Stanley, Laura-Roxana Stingaciu, Jan-Michael Y Carrillo, Bobby G Sumpter, John Katsaras, Wei Qiang and 4 more

Abstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

14 authors.

Haden L ScottDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville 37996, United States of America.
Violeta Burns-CasamayorC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, WV 26506, United States of America.
Andrew C DixsonDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville 37996, United States of America.
Robert F StandaertDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville 37996, United States of America; C. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, WV 26506, United States of America; Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, United States of America.
Christopher B StanleyShull Wollan Center - a Joint Institute for Neutron Sciences, Oak Ridge, TN 37831, United States of America; Computational Sciences and Engineering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, United States of America.
Laura-Roxana StingaciuLabs and Soft Matter Group, Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, United States of America; JCNS1, FZJ outstation at SNS, Oak Ridge National Laboratory, Oak Ridge, TN 37831, United States of America.
Jan-Michael Y CarrilloComputational Sciences and Engineering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, United States of America; Center for Nanophase Materials Sciences, Oak Ridge, TN 37831, United States of America.
Bobby G SumpterComputational Sciences and Engineering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, United States of America; Center for Nanophase Materials Sciences, Oak Ridge, TN 37831, United States of America.
John KatsarasShull Wollan Center - a Joint Institute for Neutron Sciences, Oak Ridge, TN 37831, United States of America; Labs and Soft Matter Group, Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, United States of America; Department of Physics and Astronomy, University of Tennessee, Knoxville, TN 37996, United States of America.
Wei QiangDepartment of Chemistry, the State University of New York, Binghamton, NY 13902, United States of America.
Frederick A HeberleDepartment of Chemistry, University of Tennessee, Knoxville, TN 37920, United States of America.
Blake MertzC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, WV 26506, United States of America; West Virginia University Cancer Institute, Morgantown, WV 26506, United States of America.
Rana AshkarDepartment of Physics, Virginia Tech, Blacksburg, VA 24061, United States of America; Center for Soft Matter and Biological Physics, Virginia Tech, Blacksburg, VA 24061, United States of America. Electronic address: ashkar@vt.edu.
Francisco N BarreraDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville 37996, United States of America. Electronic address: fbarrera@utk.edu.

Funding

Molecular Structural Basis of Non-specific Neuronal Membrane Disruption Induced by Early-Stage Beta-Amyloid Peptide AggregationR01GM125853 · NIGMS · STATE UNIVERSITY OF NY,BINGHAMTON · PI Wei Qiang · 2018 to 2026
$2.5M
Mechanisms of modulation of transmembrane interactionsR35GM140846 · NIGMS · UNIVERSITY OF TENNESSEE KNOXVILLE · PI BARRERA, FRANCISCO NICOLAS · 2021 to 2025
$1.9M
NIGMS NIH HHS R01 GM125853NIGMS NIH HHS R35 GM140846
6 · The paper itself

Abstract

Cell membranes are responsible for a range of biological processes that require interactions between lipids and proteins. While the effects of lipids on proteins are becoming better understood, our knowledge of how protein conformational changes influence membrane dynamics remains rudimentary. Here, we performed experiments and computer simulations to study the dynamic response of a lipid membrane to changes in the conformational state of pH-low insertion peptide (pHLIP), which transitions from a surface-associated (SA) state at neutral or basic pH to a transmembrane (TM) α-helix under acidic conditions. Our results show that TM-pHLIP significantly slows down membrane thickness fluctuations due to an increase in effective membrane viscosity. Our findings suggest a possible membrane regulatory mechanism, where the TM helix affects lipid chain conformations, and subsequently alters membrane fluctuations and viscosity.

Indexed as

Cell MembraneLipid BilayersMembrane ProteinsHydrogen-Ion ConcentrationMembrane LipidsMolecular Dynamics SimulationNeutronsViscosityLipid BilayersMembrane LipidsMembrane ProteinspHLIP proteinLipid-protein interactionsMD simulationsMembrane dynamicsMembrane viscosity

Identifiers

PMID38815687
PMCPMC11365786

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Registered trials

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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.