ArticleAmino acids2023
Effect of substituting glutamine with lysine on structural and biological properties of antimicrobial peptide Polybia-MP1.
Article in Amino acids, 2023. 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, 17 citations in OpenAlex.
- Evolution-driven terminal capping design in antimicrobial peptides revealed by combined experimental and MD simulation approaches.Archives of microbiology · 2026Article
- Influence of hydrophobicity on the antimicrobial activity of helical antimicrobial peptides: a study focusing on three mastoparans.Molecular diversity · 2025Article
- The importance role of central proline to the antimicrobial potency and selectivity of indolicidin.Archives of microbiology · 2025Article
- Reducing Self-Assembly by Increasing Net Charge: Effect on Biological Activity of Mastoparan C.ACS medicinal chemistry letters · 2024Article
- Venom-derived peptides for breaking through the glass ceiling of drug development.Frontiers in chemistry · 2024Review
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
The natural antimicrobial peptide Polybia-MP1 is a promising candidate for developing new treatment therapy for infection and cancer. It showed broad-spectrum antimicrobial and anticancer activity with high safety on healthy cells. However, previous sequence modification usually resulted in at least one of two consequences: a notable increase in hemolytic activity or a considerable decrease in activity against Gram-negative bacteria and cancer cells. Herein, a new approach was applied by replacing the amino acid Glutamine at position 12 with Lysine and generating the MP1-Q12K analog. Our preliminary data suggested an enhancement in antibacterial and antifungal activity, whereas the anticancer and hemolytic activity of the two peptides were comparable. Moreover, MP1-Q12K was found to be less self-assembly than Polybia-MP1, which further supports the enhancement of antimicrobial properties. Hence, this study provides new information regarding the structure-activity relationships of Polybia-MP1 and support for the development of potent, selective antimicrobial peptides.
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