ArticleEuropean biophysics journal : EBJ2011
Membrane interaction and antibacterial properties of two mildly cationic peptide diastereomers, bombinins H2 and H4, isolated from Bombina skin.
Article in European biophysics journal : EBJ, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 34 citations in OpenAlex.
- Biodegradable Polymers and Polymer Composites with Antibacterial Properties.International journal of molecular sciences · 2023Review
- The synergistic antimicrobial effects of novel bombinin and bombinin H peptides from the skin secretion ofBioscience reports · 2017Article
- Antimicrobial and anti-inflammatory activities of three chensinin-1 peptides containing mutation of glycine and histidine residues.Scientific reports · 2017Article
- Promising Approaches to Optimize the Biological Properties of the Antimicrobial Peptide Esculentin-1a(1-21)NHFrontiers in chemistry · 2017Review
- Feleucins: novel bombinin precursor-encoded nonapeptide amides from the skin secretion of Bombina variegata.BioMed research international · 2014Article
- Phosphatidylethanolamine binding is a conserved feature of cyclotide-membrane interactions.The Journal of biological chemistry · 2012Article
- A novel dendrimeric peptide with antimicrobial properties: structure-function analysis of SB056.Biophysical journal · 2012Article
- Isomerization of an antimicrobial peptide broadens antimicrobial spectrum to gram-positive bacterial pathogens.PloS one · 2012Article
- Tight binding of transition-state analogues to a peptidyl-aminoacyl-L/D-isomerase from frog skin.Chembiochem : a European journal of chemical biology · 2011Article
- Short native antimicrobial peptides and engineered ultrashort lipopeptides: similarities and differences in cell specificities and modes of action.Cellular and molecular life sciences : CMLS · 2011Review
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bombinins H are mildly cationic antimicrobial peptides isolated from the skin of the anuran genus Bombina, the fire-bellied toad. Some members of this peptide family coexist in skin secretions as diastereomers in which a single D: -amino acid (alloisoleucine or leucine) is incorporated as a result of the post-translational modification of the respective gene-encoded L-amino acid. Here we report on the antimicrobial properties and membrane interactions of bombinins H2 and H4. The latter differs from H2 by the presence of a D-alloisoleucine at the second N-terminal position. Specifically, we have evaluated the antimicrobial activity of H2 and H4 against a large panel of reference and clinical isolates of Gram-negative and Gram-positive bacteria; performed membrane permeation assays on both intact cells and model membranes (lipid monolayers and liposomes) mimicking the composition of the plasma membrane of Gram-negative/positive bacteria; used biochemical tools, such as trypsin-encapsulated liposomes and capillary electrophoresis, to monitor the peptides' ability to translocate through the membrane of liposomes mimicking Escherichia coli inner membrane. The results revealed interesting relationships between the presence of a single D: -amino acid in the sequence of an antimicrobial peptide and its target microbial cell selectivity/membrane-perturbing activity.
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