Evidence map›Paper›PMID 36986623›Full record

ArticlePharmaceutics2023

The Mechanism of Action of SAAP-148 Antimicrobial Peptide as Studied with NMR and Molecular Dynamics Simulations.

Morgane Adélaïde, Evgeniy Salnikov, Francisco Ramos-Martín, Christopher Aisenbrey, Catherine Sarazin, Burkhard Bechinger, Nicola D'Amelio

Abstract read
In one paragraph

Article in Pharmaceutics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Bactericidal Activity toAntibiotics (Basel, Switzerland) · 2023
    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

7 authors.

Morgane AdélaïdeUnité de Génie Enzymatique et Cellulaire UMR 7025 CNRS, Université de Picardie Jules Verne, 80039 Amiens, France.
Evgeniy SalnikovInstitut de Chimie, UMR7177, Université de Strasbourg/CNRS, 67000 Strasbourg, France.
Francisco Ramos-MartínUnité de Génie Enzymatique et Cellulaire UMR 7025 CNRS, Université de Picardie Jules Verne, 80039 Amiens, France.ORCID 0000-0002-1059-491X
Christopher AisenbreyInstitut de Chimie, UMR7177, Université de Strasbourg/CNRS, 67000 Strasbourg, France.
Catherine SarazinUnité de Génie Enzymatique et Cellulaire UMR 7025 CNRS, Université de Picardie Jules Verne, 80039 Amiens, France.
Burkhard BechingerInstitut de Chimie, UMR7177, Université de Strasbourg/CNRS, 67000 Strasbourg, France.ORCID 0000-0001-5719-6073
Nicola D'AmelioUnité de Génie Enzymatique et Cellulaire UMR 7025 CNRS, Université de Picardie Jules Verne, 80039 Amiens, France.ORCID 0000-0002-4400-2222

Funding

Agence Nationale de la Recherche NATURAL-ARSENALFederal Ministry of Education and Research NATURAL-ARSENAL
6 · The paper itself

Abstract

backgroundSAAP-148 is an antimicrobial peptide derived from LL-37. It exhibits excellent activity against drug-resistant bacteria and biofilms while resisting degradation in physiological conditions. Despite its optimal pharmacological properties, its mechanism of action at the molecular level has not been explored.

methodsThe structural properties of SAAP-148 and its interaction with phospholipid membranes mimicking mammalian and bacterial cells were studied using liquid and solid-state NMR spectroscopy as well as molecular dynamics simulations.

resultsSAAP-148 is partially structured in solution and stabilizes its helical conformation when interacting with DPC micelles. The orientation of the helix within the micelles was defined by paramagnetic relaxation enhancements and found similar to that obtained using solid-state NMR, where the tilt and pitch angles were determined based on

conclusionsSAAP-148 stabilizes its helical fold onto bacterial-like membranes, placing its helix axis almost perpendicular to the surface normal, thus probably acting by a carpet-like mechanism on the bacterial membrane rather than forming well-defined pores.

Indexed as

antimicrobialbiomembranesmembrane topologymolecular dynamicsNMRparamagnetic relaxation enhancementpeptidessolid-state NMR spectroscopy

Identifiers

PMID36986623
PMCPMC10051583

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.