ArticleScientific reports2019
Binding and Flip as Initial Steps for BP-100 Antimicrobial Actions.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed.
- A MarineMarine drugs · 2026Article
- Micellization of Zwitterionic Surfactant with Opposite Dipoles is Differently Affected by Anions.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Vesicle protrusion induced by antimicrobial peptides suggests common carpet mechanism for short antimicrobial peptides.Scientific reports · 2024Article
- Deciphering the Mechanism of Action of the Antimicrobial Peptide BP100.International journal of molecular sciences · 2024Review
- Effect of cetrimonium carrier micelles on bacterial membranes and extracellular DNA, an in silico study.Scientific reports · 2023Article
- Simulations reveal that antimicrobial BP100 induces local membrane thinning, slows lipid dynamics and favors water penetration.RSC advances · 2022Article
- Molecular dynamics study of the internalization of cell-penetrating peptides containing unnatural amino acids across membranes.Nanoscale advances · 2022Article
- Rational design of hyperstable antibacterial peptides for food preservation.NPJ science of food · 2021Article
- Naphthalimide-Containing BP100 Leads to Higher Model Membranes Interactions and Antimicrobial Activity.Biomolecules · 2021Article
- Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BP100 is a short antimicrobial peptide and can also act as a molecule-carrier into cells. Like with other antimicrobial peptides, the precise mechanism of membrane disruption is not fully understood. Here we use computer simulations to understand, at a molecular level, the initial interaction between BP100 and zwitterionic/negatively charged model membranes. In agreement with experimental results, our simulations showed BP100 folded into an alpha helix when in contact with negatively charged membranes. BP100 binding induced the aggregation of negatively charged lipids on mixed membranes composed of zwitterionic and anionic lipids. The peptide in alpha-helix conformation initially interacts with the membrane via electrostatic interactions between the negatively charged lipids and the positively charged residues of the peptide. At that point the peptide flips, burying the hydrophobic residues into the bilayer highlighting the importance of the hydrophobic effect contribution to the initial interaction of cationic antimicrobial peptides with membranes.
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Registered trials
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