Evidence map›Paper›PMID 30135402›Full record

ReviewBiomolecules2018

Membrane Active Peptides and Their Biophysical Characterization.

Fatma Gizem Avci, Berna Sariyar Akbulut, Elif Ozkirimli

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
11.6field-weighted citation impact, top 1% 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

104 citing papers in PubMed, 190 citations in OpenAlex.

  1. Review
  2. Review
  3. Covalently Linked Peptides and Membrane Potential Enable CyaA Segment Translocation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Article
  5. Membrane-Associated Biomolecules for Synthetic Cell Signalling.Chembiochem : a European journal of chemical biology · 2026
    Review
  6. KI17: A Bioinspired Peptide Derived fromMolecules (Basel, Switzerland) · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Pep5-Cpp, a Cyclin D2-Derived Antimicrobial.Molecules (Basel, Switzerland) · 2026
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Multifaceted Roles of IL-26 in Physiological and Pathological Conditions.International journal of molecular sciences · 2025
    Review
  17. Article
  18. Peptide-Based Strategies AgainstPharmaceuticals (Basel, Switzerland) · 2025
    Review
  19. Modulating Antimicrobial Activity and Structure of the Peptide Esc(1-21) via Site-Specific Isopeptide Bond Formation.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Article
  20. Article

44 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Fatma Gizem AvciBioengineering Department, Marmara University, Kadikoy, 34722 Istanbul, Turkey. gizemavci@gmail.com.ORCID 0000-0001-6618-0487
Berna Sariyar AkbulutBioengineering Department, Marmara University, Kadikoy, 34722 Istanbul, Turkey. berna.akbulut@marmara.edu.tr.ORCID 0000-0002-4455-1192
Elif OzkirimliChemical Engineering Department, Bogazici University, Bebek, 34342 Istanbul, Turkey. elif.ozkirimli@boun.edu.tr.ORCID 0000-0002-3206-8427
Marmara University · TRBoğaziçi University · TR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the last 20 years, an increasing number of studies have been reported on membrane active peptides. These peptides exert their biological activity by interacting with the cell membrane, either to disrupt it and lead to cell lysis or to translocate through it to deliver cargos into the cell and reach their target. Membrane active peptides are attractive alternatives to currently used pharmaceuticals and the number of antimicrobial peptides (AMPs) and peptides designed for drug and gene delivery in the drug pipeline is increasing. Here, we focus on two most prominent classes of membrane active peptides; AMPs and cell-penetrating peptides (CPPs). Antimicrobial peptides are a group of membrane active peptides that disrupt the membrane integrity or inhibit the cellular functions of bacteria, virus, and fungi. Cell penetrating peptides are another group of membrane active peptides that mainly function as cargo-carriers even though they may also show antimicrobial activity. Biophysical techniques shed light on peptide⁻membrane interactions at higher resolution due to the advances in optics, image processing, and computational resources. Structural investigation of membrane active peptides in the presence of the membrane provides important clues on the effect of the membrane environment on peptide conformations. Live imaging techniques allow examination of peptide action at a single cell or single molecule level. In addition to these experimental biophysical techniques, molecular dynamics simulations provide clues on the peptide⁻lipid interactions and dynamics of the cell entry process at atomic detail. In this review, we summarize the recent advances in experimental and computational investigation of membrane active peptides with particular emphasis on two amphipathic membrane active peptides, the AMP melittin and the CPP pVEC.

Indexed as

Biophysical PhenomenaAntimicrobial Cationic PeptidesCell MembraneCell-Penetrating PeptidesHumansMolecular Dynamics SimulationPeptidesAntimicrobial Cationic PeptidesCell-Penetrating PeptidesPeptidesantimicrobial peptidesbiophysical characterizationcell-penetrating peptidesmembrane disruptionpeptide–lipid interactionsuptake mechanism

Identifiers

PMID30135402
PMCPMC6164437
OpenAlexW2811376207

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.