ArticleAntimicrobial agents and chemotherapy2006
Interaction of the gelsolin-derived antibacterial PBP 10 peptide with lipid bilayers and cell membranes.
Article in Antimicrobial agents and chemotherapy, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 57 citations in OpenAlex.
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- Review
- In vitro activity of the antimicrobial peptides h-Lf1-11, MSI-78, LL-37, fengycin 2B, and magainin-2 against clinically important bacteria.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2022Article
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- Effects of Rationally Designed Physico-Chemical Variants of the Peptide PuroA on Biocidal Activity towards Bacterial and Mammalian Cells.International journal of molecular sciences · 2020Article
- Cathelicidin LL-37: A new important molecule in the pathophysiology of systemic lupus erythematosus.Journal of translational autoimmunity · 2020Review
- Peptides With Triplet-Tryptophan-Pivot Promoted Pathogenic Bacteria Membrane Defects.Frontiers in microbiology · 2020Article
- Susceptibility of microbial cells to the modified PIPJournal of nanobiotechnology · 2019Article
- The cyclic peptide labaditin does not alter the outer membrane integrity of Salmonella enterica serovar Typhimurium.Scientific reports · 2019Article
- Inhibition of inflammatory response in human keratinocytes by magnetic nanoparticles functionalized with PBP10 peptide derived from the PIP2-binding site of human plasma gelsolin.Journal of nanobiotechnology · 2019Article
- Mode of action of the antimicrobial peptide Mel4 is independent of Staphylococcus aureus cell membrane permeability.PloS one · 2019Article
- Tuning the Anti(myco)bacterial Activity of 3-Hydroxy-4-pyridinone Chelators through Fluorophores.Pharmaceuticals (Basel, Switzerland) · 2018Review
- Plasma Gelsolin: Indicator of Inflammation and Its Potential as a Diagnostic Tool and Therapeutic Target.International journal of molecular sciences · 2018Review
- Sporicidal activity of ceragenin CSA-13 against Bacillus subtilis.Scientific reports · 2017Article
- Antimicrobial Peptides Targeting Gram-Positive Bacteria.Pharmaceuticals (Basel, Switzerland) · 2016Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
PBP 10, an antibacterial, cell membrane-permeant rhodamine B-conjugated peptide derived from the polyphosphoinositide binding site of gelsolin, interacts selectively with both lipopolysaccharides (LPS) and lipoteichoic acid (LTA), the distinct components of gram-negative and gram-positive bacteria, respectively. Isolated LPS and LTA decrease the antimicrobial activities of PBP 10, as well as other antimicrobial peptides, such as cathelicidin-LL37 (LL37) and mellitin. In an effort to elucidate the mechanism of bacterial killing by PBP 10, we compared its effects on artificial lipid bilayers and eukaryotic cell membranes with the actions of the mellitin, magainin II, and LL37 peptides. This study reveals that pore formation is unlikely to be involved in PBP 10-mediated membrane destabilization. We also investigated the effects of these peptides on platelets and red blood cells (RBCs). Comparison of these antimicrobial peptides shows that only mellitin has a toxic effect on platelets and RBCs in a concentration range concomitant with its bactericidal activity. The hemolytic activities of the PBP 10 and LL37 peptides significantly increase when RBCs are osmotically swollen in hypotonic solution, indicating that these antibacterial peptides may take advantage of the more extended form of bacterial membranes in exerting their killing activities. Additionally, we found that LL37 hemolytic activity was much higher when RBCs were induced to expose phosphatidylserine to the external leaflet of their plasma membranes. This finding suggests that asymmetrical distribution of phospholipids in the external membranes of eukaryotic cells may represent an important factor in determining the specificity of antibacterial peptides for targeting bacteria rather than eukaryotic cells.
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