ArticleMolecular diversity2025
Influence of hydrophobicity on the antimicrobial activity of helical antimicrobial peptides: a study focusing on three mastoparans.
Article in Molecular diversity, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Dual-Mechanism Antimicrobial Peptides from a Nature-Inspired Scaffold.Journal of medicinal chemistry · 2026Article
- Structure-Function Insights into Anionic and Cationic Undecapeptides: A Combined Modeling and Antibacterial Study.The Journal of membrane biology · 2026Article
- Broad-Spectrum Gramicidin S Derivatives with Potent Activity Against Multidrug-Resistant Gram-Negative ESKAPE Pathogens.Antibiotics (Basel, Switzerland) · 2025Article
- The importance role of central proline to the antimicrobial potency and selectivity of indolicidin.Archives of microbiology · 2025Article
- Antimicrobial Peptides from Porcine Blood Cruor Hydrolysates as a Promising Source of Antifungal Activity.Foods (Basel, Switzerland) · 2024Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Hydrophobicity is crucial for the interaction between amphipathic antimicrobial peptides and microbial pathogens. However, it is difficult to fully understand the impact of this factor because the biological functions are also influenced by other structural properties, including peptide length, net charge, hydrophilicity, secondary structure, and hydrophobic moment. This study compares three natural antimicrobial peptides-mastoparan C, mastoparan-AF, and mastoparan L-where hydrophobicity varies but other structural features remain nearly identical. Mastoparan C, the most hydrophobic peptide, displays the highest helical content and hemolytic activity, whereas mastoparan-AF, with slightly lower hydrophobicity, demonstrates superior selectivity. In contrast, mastoparan L, the least hydrophobic peptide, exhibits the weakest antimicrobial potency and lowest hemolytic activity, despite showing the least self-assembly. Overall, this study suggests that optimal hydrophobicity, rather than the highest value, enhances antimicrobial efficacy while minimizing hemolytic activity.
Indexed as
Identifiers
39617871What OpenQuestion holds
Registered trials
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