Evidence map›Paper›PMID 30503536›Full record

ArticleBiophysical journal2018

Cooperative Nonbonded Forces Control Membrane Binding of the pH-Low Insertion Peptide pHLIP.

Chitrak Gupta, Yue Ren, Blake Mertz

Open access · bronzeAbstract 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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Small animal PET imaging with theEJNMMI radiopharmacy and chemistry · 2024
    Article
  4. Arginine Residues Modulate the Membrane Interactions of pHLIP Peptides.Journal of chemical information and modeling · 2023
    Article
  5. pHLIP Peptides Target Acidity in Activated Macrophages.Molecular imaging and biology · 2022
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. 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

3 authors at 1 institution in 1 country.

Chitrak GuptaC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, West Virginia.
Yue RenC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, West Virginia.
Blake MertzC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, West Virginia. Electronic address: blake.mertz@mail.wvu.edu.
West Virginia University · US

Funding

Optimizing pHLIP: understanding biophysical interactions of membrane insertionR15GM120676 · NIGMS · WEST VIRGINIA UNIVERSITY · PI MERTZ, BLAKE · 2016 to 2016
$414k
NIGMS NIH HHS R15 GM120676
6 · The paper itself

Abstract

Peptides with the ability to bind and insert into the cell membrane have immense potential in biomedical applications. pH (low) insertion peptide (pHLIP), a water-soluble polypeptide derived from helix C of bacteriorhodopsin, can insert into a membrane at acidic pH to form a stable transmembrane α-helix. The insertion process takes place in three stages: pHLIP is unstructured and soluble in water at neutral pH (state I), unstructured and bound to the surface of a membrane at neutral pH (state II), and inserted into the membrane as an α-helix at low pH (state III). Using molecular dynamics simulations, we have modeled state II of pHLIP and a fast-folding variant of pHLIP, in which each peptide is bound to a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine bilayer surface. Our results provide strong support for recently published spectroscopic studies, namely that pHLIP preferentially binds to the bilayer surface as a function of location of anionic amino acids and that backbone dehydration occurs upon binding. Unexpectedly, we also observed several instances of segments of pHLIP folding into a stable helical turn. Our results provide a molecular level of detail that is essential to providing new insights into pHLIP function and to facilitate design of variants with improved membrane-active capabilities.

Indexed as

Mechanical PhenomenaAmino Acid SequenceBiomechanical PhenomenaCell MembraneMembrane ProteinsMolecular Dynamics SimulationProtein BindingProtein Conformation, alpha-HelicalMembrane ProteinspHLIP protein

Identifiers

PMID30503536
PMCPMC6301916
OpenAlexW2951522718

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.