Evidence map›Paper›PMID 32988206›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2020

Using Simulation to Understand the Role of Titration on the Stability of a Peptide-Lipid Bilayer Complex.

Violetta Burns, Blake Mertz

Abstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Increasing the Realism ofJournal of chemical theory and computation · 2022
    Article
  2. CaProtein science : a publication of the Protein Society · 2022
    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

2 authors.

Violetta BurnsC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, West Virginia 26506, United States.
Blake MertzC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, West Virginia 26506, United States.ORCID 0000-0002-7677-0496

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

The pH-low insertion peptide (pHLIP) is an anionic membrane-active peptide with promising potential for applications in imaging of cancer tumors and targeted delivery of chemotherapeutics. The key advantage of pHLIP lies in its acid sensitivity: in acidic cellular environments, pHLIP can insert unidirectionally into the plasma membrane. Partitioning-folding coupling is triggered by titration of the acidic residues in pHLIP, transforming pHLIP from a hydrophilic to a hydrophobic peptide. Despite this knowledge, the reverse pathway that leads to exit of the peptide from the plasma membrane is poorly understood. Our hypothesis is that sequential deprotonation of pHLIP is a prerequisite for exit of the peptide from the plasma membrane. We carried out molecular dynamics (MD) simulations to characterize the effect that deprotonation of the acidic residues of pHLIP has on the stability of the peptide when inserted into a model lipid bilayer of 1-palmitoyl-2-oleoyl-

Indexed as

Lipid BilayersPeptidesCell MembraneHydrogen-Ion ConcentrationProtein Structure, SecondaryLipid BilayersPeptides

Identifiers

PMID32988206
PMCPMC7778881

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.