Evidence map›Paper›PMID 25692583›Full record

ArticleBiophysical journal2015

Lipid headgroups modulate membrane insertion of pHLIP peptide.

Alexander Kyrychenko, Victor Vasquez-Montes, Martin B Ulmschneider, Alexey S Ladokhin

Open access · bronzeAbstract 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 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

36 citing papers in PubMed, 62 citations in OpenAlex.

  1. Improving the Estimation of pThe journal of physical chemistry. B · 2026
    Article
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  6. Review
  7. Review
  8. Article
  9. Arginine Residues Modulate the Membrane Interactions of pHLIP Peptides.Journal of chemical information and modeling · 2023
    Article
  10. Oriented Insertion of ESR-Containing Hybrid Proteins in Proteoliposomes.International journal of molecular sciences · 2023
    Article
  11. pHLIP Peptides Target Acidity in Activated Macrophages.Molecular imaging and biology · 2022
    Article
  12. Increasing the Realism ofJournal of chemical theory and computation · 2022
    Article
  13. CaProtein science : a publication of the Protein Society · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Pharmacokinetic modeling reveals parameters that govern tumor targeting and delivery by a pH-Low Insertion Peptide (pHLIP).Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Article
  19. How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020
    Review
  20. 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

4 authors at 2 institutions in 1 country.

Alexander KyrychenkoDepartment of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, Kansas.
Victor Vasquez-MontesDepartment of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, Kansas.
Martin B UlmschneiderDepartment of Materials Science and Engineering, Johns Hopkins University, Baltimore, Maryland.
Alexey S LadokhinDepartment of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, Kansas. Electronic address: aladokhin@kumc.edu.
University of Kansas Medical Center · USJohns Hopkins University · US

Funding

pH-Triggered Membrane Insertion of ProteinsR01GM069783 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI COCCO, MELANIE J, KURNIKOVA, MARIA G · 2004 to 2014
$2.5M
NIGMS NIH HHS GM-069783NIGMS NIH HHS R01 GM069783
6 · The paper itself

Abstract

The pH low insertion peptide (pHLIP) is an important tool for drug delivery and visualization of acidic tissues produced by various maladies, including cancer, inflammation, and ischemia. Numerous studies indicate that pHLIP exists in three states: unfolded and soluble in water at neutral pH (State I), unfolded and bound to the surface of a phosphatidylcholine membrane at neutral pH (State II), and inserted across the membrane as an α-helix at low pH (State III). Here we report how changes in lipid composition modulate this insertion scheme. First, the presence of either anionic lipids, cholesterol, or phosphoethanolamine eliminates membrane binding at neutral pH (State II). Second, the apparent pKa for the insertion transition (State I → State III) is increased with increasing content of anionic lipids, suggesting that electrostatic interactions in the interfacial region modulate protonation of acidic residues of pHLIP responsible for transbilayer insertion. These findings indicate a possibility for triggering protonation-coupled conformational switching in proteins at membrane interfaces through changes in lipid composition.

Indexed as

Amino Acid SequenceCholesterolEthanolaminesLipid BilayersMembrane ProteinsMolecular Sequence DataStatic ElectricityCholesterolEthanolaminesLipid BilayersMembrane ProteinspHLIP proteinphosphorylethanolamine

Identifiers

PMID25692583
PMCPMC4336367
OpenAlexW2056872913

What OpenQuestion 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 OpenQuestion graph.