Evidence map›Paper›PMID 27726396›Full record

ArticleThe journal of physical chemistry. B2016

pHLIP Peptide Interaction with a Membrane Monitored by SAXS.

Theyencheri Narayanan, Dhammika Weerakkody, Alexander G Karabadzhak, Michael Anderson, Oleg A Andreev, Yana K Reshetnyak

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Discovery of Kinetic Trapping of Poloxamers inside Liposomes via Thermal Treatment.Langmuir : the ACS journal of surfaces and colloids · 2023
    Article
  7. Review
  8. Arginine Residues Modulate the Membrane Interactions of pHLIP Peptides.Journal of chemical information and modeling · 2023
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Cancer targeting peptides.Cellular and molecular life sciences : CMLS · 2019
    Review
  18. Article
  19. Review
  20. Analysis of Trisiloxane Phosphocholine Bilayers.Langmuir : the ACS journal of surfaces and colloids · 2017
    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 at 2 institutions in 2 countries.

Theyencheri NarayananESRF - The European Synchrotron , 38043 Grenoble, France.
Dhammika WeerakkodyDepartment of Physics, University of Rhode Island , Kingston, Rhode Island 02881, United States.
Alexander G KarabadzhakDepartment of Physics, University of Rhode Island , Kingston, Rhode Island 02881, United States.
Michael AndersonDepartment of Physics, University of Rhode Island , Kingston, Rhode Island 02881, United States.
Oleg A AndreevDepartment of Physics, University of Rhode Island , Kingston, Rhode Island 02881, United States.
Yana K ReshetnyakDepartment of Physics, University of Rhode Island , Kingston, Rhode Island 02881, United States.
University of Rhode Island · USEuropean Synchrotron Radiation Facility · FR

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

pH (Low) Insertion Peptides (pHLIP peptides) find application in studies of membrane-associated folding because spontaneous insertion of these peptides is conveniently triggered by varying pH. Here, we employed small-angle X-ray scattering (SAXS) to investigate a wild-type (WT) pHLIP peptide oligomeric state in solution at high concentrations and monitor changes in the liposome structure upon peptide insertion into the bilayer. We established that even at high concentrations (up to 300 μM) the WT pHLIP peptide at pH 8.0 does not form oligomers larger than tetramers (which exhibit concentration-dependent transfer to the monomeric state, as was shown previously). This finding has significance for medical applications when high concentration of the peptide is injected into blood and diluted in blood circulation. The interaction of WT pHLIP peptide with liposomes does not alter the unilamellar vesicle structure upon peptide adsorption by the lipid bilayer at high pH or upon insertion across the bilayer at low pH. At the same time, SAXS data clearly demonstrate the insertion of the peptide into the membrane at low pH, which opens the possibility of investigating the kinetic process of polypeptide insertion and exit from the membrane in real time by time-resolved SAXS.

Indexed as

AdsorptionHydrogen-Ion ConcentrationLipid BilayersLiposomesMembrane ProteinsScattering, Small AngleX-Ray DiffractionLipid BilayersLiposomesMembrane ProteinspHLIP protein

Identifiers

PMID27726396
PMCPMC5209755
OpenAlexW2530267922

What Socratic holds

Textmetadata
LicenceTDM
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.