ArticleScientific reports2017
Structure and membrane interactions of the homodimeric antibiotic peptide homotarsinin.
Article in Scientific reports, 2017. 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 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.
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- The Synthetic Peptide LyeTx I mn∆K, Derived fromAntibiotics (Basel, Switzerland) · 2024Article
- Expanding the genomic encyclopedia ofCell genomics · 2022Article
- Synthetic Peptides Derived FromFrontiers in molecular biosciences · 2021Article
- Heterodimeric Insecticidal Peptide Provides New Insights into the Molecular and Functional Diversity of Ant Venoms.ACS pharmacology & translational science · 2020Article
- Revealing the Mechanisms of Synergistic Action of Two Magainin Antimicrobial Peptides.Frontiers in medical technology · 2020Review
- Antibacterial and Antibiofilm Activity of Temporin-GHc and Temporin-GHd Against Cariogenic Bacteria,Frontiers in microbiology · 2019Article
- Identification, Recombinant Expression, and Characterization of LHG2, a Novel Antimicrobial Peptide ofMolecules (Basel, Switzerland) · 2018Article
- Synergism of Antimicrobial Frog Peptides Couples to Membrane Intrinsic Curvature Strain.Biophysical journal · 2018Article
- Biophysical Investigations Elucidating the Mechanisms of Action of Antimicrobial Peptides and Their Synergism.Biomolecules · 2018Review
- LyeTxI-b, a Synthetic Peptide Derived FromFrontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antimicrobial peptides (AMPs) from amphibian skin are valuable template structures to find new treatments against bacterial infections. This work describes for the first time the structure and membrane interactions of a homodimeric AMP. Homotarsinin, which was found in Phyllomedusa tarsius anurans, consists of two identical cystine-linked polypeptide chains each of 24 amino acid residues. The high-resolution structures of the monomeric and dimeric peptides were determined in aqueous buffers. The dimer exhibits a tightly packed coiled coil three-dimensional structure, keeping the hydrophobic residues screened from the aqueous environment. An overall cationic surface of the dimer assures enhanced interactions with negatively charged membranes. An extensive set of biophysical data allowed us to establish structure-function correlations with antimicrobial assays against Gram-positive and Gram-negative bacteria. Although both peptides present considerable antimicrobial activity, the dimer is significantly more effective in both antibacterial and membrane biophysical assays.
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Registered trials
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.