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Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
The effects of magainin 2-derived and rationally designed antimicrobial peptides on Mycoplasma pneumoniae
Katsuhiko Hayashi1, Takashi Misawa2, Chihiro Goto3
1Division of Microbiology, National Institute of Health Sciences, Kawasaki, Kanagawa, Japan.
Abstract:
Combating the spread of antimicrobial resistance (AMR) among bacteria requires a new class of antimicrobials, which desirably have a narrow spectrum because of their low propensity for the spread of AMR. Antimicrobial peptides (AMPs), which target the bacterial cell membrane, are promising seeds for novel antimicrobials because the cell membrane is essential for all cells. Previously, we reported the antimicrobial and haemolytic effects of a natural AMP, magainin 2 (Mag2), isolated from the skin of Xenopus laevis (the African clawed frog), four types of synthesised Mag2 derivatives, and three types of rationally designed AMPs on gram-positive and gram-negative bacteria. To identify novel antimicrobial seeds, we evaluated the effect of AMPs on Mycoplasma pneumoniae, which also exhibits AMR. We also evaluated the antimicrobial effects of an AMP, NK2A, which has been reported to have antimicrobial effects on Mycoplasma bovis, in addition to Mag2 and previously synthesised seven AMPs, on four strains of M. pneumoniae using colorimetric, biofilm, and killing assays. We found that three synthesised AMPs, namely 17base-Ac6c, 17base-Hybrid, and Block, had anti-M. pneumoniae (anti-Mp) effect at 8-30 μM, whereas others, including NK2A, did not have any such effect. For the further analysis, the membrane disruption activities of AMPs were measured by propidium iodide (PI) uptake assays, which suggested the direct interaction of AMPs to the cell membrane basically following the colorimetric, biofilm, and killing assay results. PI uptake assay, however, also showed the NK2A strong interaction to cell membrane, indicating unknown anti-Mp determinant factors related to the peptide sequences. Finally, we conclude that anti-Mp effect was not simply determined by the membrane disruption activities of AMPs, but also that the sequence of AMPs were important for killing of M. pneumoniae. These findings would be helpful for the development of AMPs for M. pneumoniae.
Insights
Three synthesized antimicrobial peptides (AMPs) show efficacy against Mycoplasma pneumoniae, demonstrating that peptide sequence, not just membrane disruption, is key for combating antimicrobial resistance (AMR).
Area of Science:
- Microbiology
- Biochemistry
- Drug Discovery
Background:
- Antimicrobial resistance (AMR) necessitates novel antimicrobials with narrow-spectrum activity to limit resistance spread.
- Antimicrobial peptides (AMPs) targeting the essential bacterial cell membrane are promising candidates for new drugs.
- Previous studies evaluated magainin 2 (Mag2) derivatives and designed AMPs against Gram-positive and Gram-negative bacteria.
Purpose of the Study:
- To identify novel antimicrobial peptide (AMP) seeds effective against Mycoplasma pneumoniae, a bacterium exhibiting AMR.
- To evaluate the anti-M. pneumoniae (anti-Mp) activity of Mag2 and seven previously synthesized AMPs, including NK2A.
- To investigate the relationship between AMP membrane disruption and anti-M. pneumoniae efficacy.
Main Methods:
- Colorimetric, biofilm, and killing assays were used to assess AMP activity against four M. pneumoniae strains.
- Propidium iodide (PI) uptake assays measured membrane disruption capabilities of the AMPs.
- Comparative analysis of AMP efficacy and membrane interaction was performed.
Main Results:
- Three synthesized AMPs (17base-Ac6c, 17base-Hybrid, Block) exhibited anti-M. pneumoniae activity at 8-30 μM.
- Other tested AMPs, including NK2A, showed no significant anti-M. pneumoniae effect.
- While PI uptake indicated NK2A interacts with the cell membrane, it lacked anti-M. pneumoniae efficacy, suggesting sequence-dependent factors are crucial.
Conclusions:
- Antimicrobial peptide efficacy against M. pneumoniae is not solely determined by membrane disruption.
- The specific amino acid sequence of AMPs plays a critical role in their activity against M. pneumoniae.
- These findings provide insights for developing novel AMPs targeting M. pneumoniae and combating AMR.
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