Evidence map›Paper›PMID 29742404›Full record

ArticleBiophysical journal2018

Bilayer Thickness and Curvature Influence Binding and Insertion of a pHLIP Peptide.

Alexander G Karabadzhak, Dhammika Weerakkody, John Deacon, Oleg A Andreev, Yana K Reshetnyak, Donald M Engelman

Abstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. pHLIP Peptides Target Acidity in Activated Macrophages.Molecular imaging and biology · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Kinetics of pHLIP peptide insertion into and exit from a membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. A How-To Guide for Mode of Action Analysis of Antimicrobial Peptides.Frontiers in cellular and infection microbiology · 2020
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
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.

Alexander G KarabadzhakDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut.
Dhammika WeerakkodyPhysics Department, University of Rhode Island, Kingston, Rhode Island.
John DeaconDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut.
Oleg A AndreevPhysics Department, University of Rhode Island, Kingston, Rhode Island.
Yana K ReshetnyakPhysics Department, University of Rhode Island, Kingston, Rhode Island. Electronic address: reshetnyak@uri.edu.
Donald M EngelmanDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut. Electronic address: donald.engelman@yale.edu.

Funding

TM INTERACTIONS IN MEMBRANE PROTEIN FOLDING AND FUNCTIONR01GM073857 · NIGMS · YALE UNIVERSITY · PI ANDREEV, OLEG A, ENGELMAN, DONALD M. · 2006 to 2023
$8.4M
NIGMS NIH HHS R01 GM073857
6 · The paper itself

Abstract

The physical properties of lipid bilayers, such as curvature and fluidity, can affect the interactions of polypeptides with membranes, influencing biological events. Additionally, given the growing interest in peptide-based therapeutics, understanding the influence of membrane properties on membrane-associated peptides has potential utility. pH low insertion peptides (pHLIPs) are a family of water-soluble peptides that can insert across cell membranes in a pH-dependent manner, enabling the use of pH to follow peptide-lipid interactions. Here we study pHLIP interactions with liposomes varying in size and composition, to determine the influence of several key membrane physical properties. We find that pHLIP binding to bilayer surfaces at neutral pH is governed by the ease of access to the membrane's hydrophobic core, which can be facilitated by membrane curvature, thickness, and the cholesterol content of the membrane. After surface binding, if the pH is lowered, the kinetics of pHLIP folding to form a helix and subsequent insertion across the membrane depends on the fluidity and energetic dynamics of the membrane. We showed that pHLIP is capable of forming a helix across lipid bilayers of different thicknesses at low pH. However, the kinetics of the slow phase of insertion corresponding to the translocation of C-terminal end of the peptide across lipid bilayer, vary approximately twofold, and correlate with bilayer thickness and fluidity. Although these influences are not large, local curvature variations in membranes of different fluidity could selectively influence surface binding in mixed cell populations.

Indexed as

Hydrogen-Ion ConcentrationLipid BilayersLiposomesMembrane ProteinsPhosphatidylcholinesProtein BindingSurface PropertiesLipid BilayersLiposomesMembrane ProteinspHLIP proteinPhosphatidylcholines

Identifiers

PMID29742404
PMCPMC5961746

What OpenQuestion holds

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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.