Evidence map›Paper›PMID 31683755›Full record

ArticleInternational journal of molecular sciences2019

Self-Association of Antimicrobial Peptides: A Molecular Dynamics Simulation Study on Bombinin.

Peicho Petkov, Elena Lilkova, Nevena Ilieva, Leandar Litov

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. A MarineMarine drugs · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Antimicrobial Peptides: From Design to Clinical Application.Antibiotics (Basel, Switzerland) · 2022
    Review
  11. Review
  12. Antimicrobial Peptides: An Update on Classifications and Databases.International journal of molecular sciences · 2021
    Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Aggregation State of Synergistic Antimicrobial Peptides.The journal of physical chemistry letters · 2020
    Article
  18. Designer Biopolymers: Self-Assembling Proteins and Nucleic Acids.International journal of molecular sciences · 2020
    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

4 authors.

Peicho PetkovFaculty of Physics, Atomic Physics Department, Sofia University "St. Kliment Ohridski", 5 J. Bouchier Blvd, 1164 Sofia, Bulgaria. peicho@phys.uni-sofia.bg.ORCID 0000-0002-0420-9480
Elena LilkovaInstitute of Information and Communication Technologies at the Bulgarian Academy of Sciences, Acad. G. Bonchev Str., Block 25A, 1113 Sofia, Bulgaria. elilkova@parallel.bas.bg.ORCID 0000-0003-2008-710X
Nevena IlievaInstitute of Information and Communication Technologies at the Bulgarian Academy of Sciences, Acad. G. Bonchev Str., Block 25A, 1113 Sofia, Bulgaria. nevena.ilieva@parallel.bas.bg.ORCID 0000-0002-2372-2319
Leandar LitovFaculty of Physics, Atomic Physics Department, Sofia University "St. Kliment Ohridski", 5 J. Bouchier Blvd, 1164 Sofia, Bulgaria. Leandar.Litov@cern.ch.ORCID 0000-0002-8511-6883

Funding

Bulgarian National Science Fund KP-06-OPR 03-10/2018Ministry of Education, Youth and Science D01-217/30.11.2018, DCM # 658/14.09.2018
6 · The paper itself

Abstract

Antimicrobial peptides (AMPs) are a diverse group of membrane-active peptides which play a crucial role as mediators of the primary host defense against microbial invasion. Many AMPs are found to be fully or partially disordered in solution and to acquire secondary structure upon interaction with a lipid membrane. Here, we report molecular dynamics simulations studies on the solution behaviour of a specific AMP, bombinin H2. We show that in monomeric form in water solution the peptide is somewhat disordered and preferably adopts a helix-loop-helix conformation. However, when more than a single monomer is placed in the solution, the peptides self-associate in aggregates. Within the aggregate, the peptides provide each other with an amphipathic environment that mimics the water-membrane interface, which allows them to adopt a single-helix structure. We hypothesise that this is the mechanism by which bombinin H2 and, possibly, other small linear AMPs reach the target membrane in a functional folded state and are able to effectively exert their antimicrobial action on it.

Indexed as

Molecular Dynamics SimulationProtein Structure, SecondaryAntimicrobial Cationic PeptidesMembrane LipidsProtein BindingWaterAntimicrobial Cationic Peptidesbombinin H2Membrane LipidsWateraggregationantimicrobial peptidespromotion of foldingself-association

Identifiers

PMID31683755
PMCPMC6862524

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Registered trials

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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.