Evidence map›Paper›PMID 39532898›Full record

ArticleScientific reports2024

Computational investigation of the effect of BODIPY labelling on peptide-membrane interaction.

Dominique de Jong-Hoogland, Jacob Ulmschneider, Martin Ulmschneider

Abstract read
In one paragraph

Article in Scientific reports, 2024. 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. A nanoscale Jitterbug transformer from DNA.Nature communications · 2026
    Article
  2. 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.

Dominique de Jong-HooglandDepartment of Chemistry, King's College London, London, UK. dominique.hoogland@kcl.ac.uk.ORCID 0000-0002-1655-2833
Jacob UlmschneiderInstitute of Natural Sciences, Shanghai Jiao Tong University, Shanghai, China. jakob@sjtu.edu.cn.
Martin UlmschneiderDepartment of Chemistry, King's College London, London, UK.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Optical monitoring of peptide binding to live cells is hampered by the abundance of naturally occurring fluorophores such as tryptophan. Unnatural amino acids incorporating synthetic fluorophores such as BODIPY overcome these optical limitations. A drawback to using fluorophores in lipid binding peptide design is their propensity to override other interactions, potentially causing the peptides to lose their binding selectivity. Here, the binding strength of a selection of peptides incorporating a variety of BODIPY derivatized amino acids has been studied via molecular dynamics simulations to quantify the impact of BODIPY incorporation on peptide-membrane binding behaviour.

Indexed as

Boron CompoundsMolecular Dynamics SimulationPeptidesAmino AcidsCell MembraneFluorescent DyesProtein Binding4,4-difluoro-4-bora-3a,4a-diaza-s-indaceneAmino AcidsBoron CompoundsFluorescent DyesPeptidesBODIPYdeltaGMembrane active peptideMolecular dynamic simulations

Identifiers

PMID39532898
PMCPMC11557973

What OpenQuestion holds

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LicenceCC BY
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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.