ArticleAmino acids2022
Fast killing kinetics, significant therapeutic index, and high stability of melittin-derived antimicrobial peptide.
Article in Amino acids, 2022. 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, 15 citations in OpenAlex.
- A Localization-Based Motif Combination Approach To the Design of Antimicrobial Peptides Targeting Gram-Positive and Gram-Negative Bacteria.Probiotics and antimicrobial proteins · 2026Article
- Article
- Bee Venom and Cancer: A Mini-review Focusing on Melittin Antitumoral Effects.Current drug targets · 2026Review
- Therapeutic Bioactivity Exerted by theMolecules (Basel, Switzerland) · 2025Article
- In Vitro and In Vivo Evaluation of the De Novo Designed Antimicrobial Peptide P6.2 Against a KPC-ProducingBiomolecules · 2025Article
- Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides.PloS one · 2025Article
- Intracellular bactericidal activity and action mechanism of MDP1 antimicrobial peptide against VRSA and MRSA in human endothelial cells.Frontiers in microbiology · 2024Article
- Rapid eradication of vancomycin and methicillin-resistantFrontiers in bioengineering and biotechnology · 2024Article
- Computationally Designed AMPs with Antibacterial and Antibiofilm Activity against MDRAntibiotics (Basel, Switzerland) · 2023Article
- Antibiofilm effect of melittin alone and in combination with conventional antibiotics toward strong biofilm of MDR-MRSA and -Frontiers in microbiology · 2023Article
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The emergence of multidrug-resistant (MDR) bacteria is a major challenge for antimicrobial chemotherapy. Concerning this issue, antimicrobial peptides (AMPs) have been presented as novel promising antibiotics. Our previous de novo designed melittin-derived peptides (MDP1 and MDP2) indicated their potential as peptide drug leads. Accordingly, this study was aimed to evaluate the kinetics of activity, toxicity, and stability of MDP1 and MDP2 as well as determination of their structures. The killing kinetics of MDP1 and MDP2 demonstrate that all bacterial strains were rapidly killed. MDP1 and MDP2 were ca. 100- and 26.6-fold less hemolytic than melittin and found to be respectively 72.9- and 41.6-fold less cytotoxic than melittin on the HEK293 cell line. MDP1 and MDP2 showed 252- and 132-fold improvement in their therapeutic index in comparison to melittin. MDP1 and MDP2 sustained their activities in the presence of human plasma and were found to be ca. four to eightfold more stable than melittin. Spectropolarimetry analysis of MDP1 and MDP2 indicates that the peptides adopt an alpha-helical structure predominantly. According to the fast killing kinetics, significant therapeutic index, and high stability of MDP1, it could be considered as a drug lead in a mouse model of septicemia infections.
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