Difference between revisions of "Part:BBa K4147001"
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<partinfo>BBa_K4147001 short</partinfo>
 
<partinfo>BBa_K4147001 short</partinfo>
  
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Among a wide range of AMPs, polycationic dermaseptin peptides are produced by the skin glands of the frog <i>Phyllomedusa bicolor</i>[1]. It supplies both antibacterial and antifungal protection to a broad range of plant pathogens but shows no toxic effects on plant and mammalian cells [1]. This 3.2 kDa peptide contains a tandem repeat of a chitin binding domain (CBD) from <i>Cladosporium fulvum</i>as an improvement of dermaseptin-b1 gene (AKA MsrA2)(BBa_K2577001) which binds to chitin fungal cell wall, thereby increasing the lytic activity of the catalytic domain. The peptide is fused with a PelB sequence (BBa_J32015) to send the protein to periplasmic space for an easier purification. The sequence also contains a 6xHis tag for purification with IMAC.
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Among a wide range of AMPs, polycationic dermaseptin peptides are produced by the skin glands of the frog <i>Phyllomedusa bicolor</i>[1]. It supplies both antibacterial and antifungal protection to a broad range of plant pathogens but shows no toxic effects on plant and mammalian cells [1]. This 3.2 kDa peptide contains a tandem repeat of a chitin binding domain (CBD) from <i>Cladosporium fulvum</i>as an improvement of dermaseptin-b1 gene (AKA MsrA2)(BBa_K2577001) which binds to chitin fungal cell wall, thereby increasing the lytic activity of the catalytic domain. The peptide is fused with a PelB sequence (BBa_J32015) to send the protein to periplasmic space for an easier purification. The sequence also contains a 6xHis tag for purification with IMAC. The final protein has a molecular mass of 25.1 kDa
  
  

Revision as of 05:47, 8 October 2022


PelB-(CBD)2-DrsB1: A dermaseptin antimicrobial peptide from Phyllomedusa bicolor

Among a wide range of AMPs, polycationic dermaseptin peptides are produced by the skin glands of the frog Phyllomedusa bicolor[1]. It supplies both antibacterial and antifungal protection to a broad range of plant pathogens but shows no toxic effects on plant and mammalian cells [1]. This 3.2 kDa peptide contains a tandem repeat of a chitin binding domain (CBD) from Cladosporium fulvumas an improvement of dermaseptin-b1 gene (AKA MsrA2)(BBa_K2577001) which binds to chitin fungal cell wall, thereby increasing the lytic activity of the catalytic domain. The peptide is fused with a PelB sequence (BBa_J32015) to send the protein to periplasmic space for an easier purification. The sequence also contains a 6xHis tag for purification with IMAC. The final protein has a molecular mass of 25.1 kDa


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 165
    Illegal AgeI site found at 444
  • 1000
    COMPATIBLE WITH RFC[1000]


References

[1] Khademi, M., Varasteh-Shams, M., Nazarian-Firouzabadi, F., & Ismaili, A. (2020). New Recombinant Antimicrobial Peptides Confer Resistance to Fungal Pathogens in Tobacco Plants. Frontiers in plant science, 11, 1236. https://doi.org/10.3389/fpls.2020.01236