ArticlePloS one2019
Structural characterization of scorpion peptides and their bactericidal activity against clinical isolates of multidrug-resistant bacteria.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Antimicrobial Peptides Targeting Salmonella enterica serovar Typhi: Mechanism of Action, Structural Insights, and Translational Challenges - A Review.Probiotics and antimicrobial proteins · 2026Review
- Article
- Designing a Potent, Low-Toxicity Antimicrobial Peptide Inspired by Scorpion Peptides: Optimizing Expression and Activity.Probiotics and antimicrobial proteins · 2026Article
- Structural determinants of the scorpion venom peptide Uy234 govern bactericidal activity and membrane-disruptive properties.Frontiers in microbiology · 2026Article
- Review
- Molecular dynamics study of the helix-to-disorder transition in short antimicrobial peptides from Urodacus yaschenkoi.European biophysics journal : EBJ · 2025Article
- The Role of Flexibility in the Bioactivity of Short α-Helical Antimicrobial Peptides.Antibiotics (Basel, Switzerland) · 2025Review
- Combating Antibiotic Resistance: Mechanisms, Multidrug-Resistant Pathogens, and Novel Therapeutic Approaches: An Updated Review.Pharmaceuticals (Basel, Switzerland) · 2025Review
- The inhibitory potential of three scorpion venom peptides against multidrug-resistantFrontiers in microbiology · 2025Article
- Antimicrobial Potential of Scorpion-Venom-Derived Peptides.Molecules (Basel, Switzerland) · 2024Review
- A Critical Review of Short Antimicrobial Peptides from Scorpion Venoms, Their Physicochemical Attributes, and Potential for the Development of New Drugs.The Journal of membrane biology · 2024Review
- QSAR Reveals Decreased Lipophilicity of Polar Residues Determines the Selectivity of Antimicrobial Peptide Activity.ACS omega · 2024Article
- Evaluation of the activity of antimicrobial peptides against bacterial vaginosis.Open life sciences · 2024Article
- Scorpion Venom as a Source of Antimicrobial Peptides: Overview of Biomolecule Separation, Analysis and Characterization Methods.Antibiotics (Basel, Switzerland) · 2023Review
- Peptidomics.Nature reviews. Methods primers · 2023Article
- The evolutionary diversification and antimicrobial potential of MPEG1 in Metazoa.Computational and structural biotechnology journal · 2023Article
- Review
- Heterogeneous-Backbone Proteomimetic Analogues of Lasiocepsin, a Disulfide-Rich Antimicrobial Peptide with a Compact Tertiary Fold.ACS chemical biology · 2022Article
- In Silico and In Vitro Structure-Activity Relationship of Mastoparan and Its Analogs.Molecules (Basel, Switzerland) · 2022Article
- TanP: A Multifunctional Anionic Peptide FromFrontiers in molecular biosciences · 2021Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Scorpion venom peptides represent a novel source of antimicrobial peptides (AMPs) with broad-spectrum activity. In this study, we determined the minimum bactericidal concentration (MBC) of three scorpion AMPs, Uy234, Uy17, and Uy192, which are found in the venomous glands of the Urodacus yaschenkoi scorpion, against the clinical isolates of multidrug-resistant (MDR) bacteria. In addition, we tested the activity of a consensus AMP designed in our laboratory based on some previously reported IsCT-type (cytotoxic linear peptide) AMPs with the aim of obtaining higher antimicrobial activity. All peptides tested showed high antimicrobial activity against MDR clinical isolates, with the highest activity against β-hemolytic Streptococcus strains. The hemolytic activity was determined against human red blood cells and was significantly lower than that of previously reported AMPs. The α-helical structure of the four AMPs was confirmed by circular dichroism (CD). These results suggest that the four peptides can be valuable tools for the design and development of AMPs for use in the inhibition of MDR pathogenic bacteria. A clear index of synergism and additivity was found for the combination of QnCs-BUAP + Uy234, which makes these peptides the most promising candidates against pathogenic bacteria.
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