• DRAMP ID

    • DRAMP18194
    • Peptide Name

    • AAEL000598-PA
    • Source

    • Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
    • Family

    • Unknow
    • Gene

    • CECD
    • Sequence

    • GGLKKLGKKLEGAGKRVFKASEKALPVVVGIKAIGK
    • Sequence Length

    • 36
    • Evidence code

    • Biological Activity

    • Antibacterial
    • Target Organism

      • Gram-negative (including drug-resistent): E. coli (MIC 2-4 ug/mL), P. aeruginosa (MIC 1-4 ug/mL), A. baumannii (MIC 1-2 ug/mL), K. pneunomiae (MIC 1-2 ug/mL).
      • No antibacterial effects of the peptide were observed against different isolates of Gram-positive S. aureus, E. faecalis and E. faecium strains showing MIC values over 32. (Pubmed:25162372)
    • Hemolytic activity

    • Unknown
    • Binding Traget

    • Unknow
    • Structure

    • alpha helical (N-terminal)
    • Structure Description

    • The structure of Aedesin is depicted as a helix-bent-helix structure with good RMSD statistics for the N-terminal helix (helix 1) and for the C-terminal helix (helix 2) taken separately.The helical wheel diagram of Aedesin shows the amphipathic character of the first and second aloha helices, as well as the opposite localization of their hydrophobic and positively charged residues, respectively.
    • PDB ID

    • 2MMM resolved by NMR.
    • DRAMP18194 helical wheel diagram
    • 2MMM-> 
    • Formula

    • C169H300N48O42
    • Absent Amino Acids

    • CDHMNQTWY
    • Common Amino Acids

    • K
    • Mass

    • 430103
    • PI

    • 11.33
    • Basic Residues

    • 10
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 15
    • Boman Index

    • -1941
    • Hydrophobicity

    • -2.22
    • Aliphatic Index

    • 108.33
    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 8

Amino Acid Distribution

DRAMP18194 chydropathy plot
    • The anti-bacterial activity of Aedesin was found to be salt-resistant, indicating that it is active under physiological conditions encountered in body fluids characterized by ionic salt concentrations.

  • Literature 1
    • Reference

    • Science 316:1718-1723(2007).
    • Author

    • Nene V., Wortman J.R., Lawson D., et al.
    • Title

    • Genome sequence of Aedes aegypti, a major arbovirus vector.
  • Literature 2
    • Reference

    • PLoS ONE 9:e105441-e105441(2014).
    • Author

    • Godreuil S., Leban N., Padilla A., et al.
    • Title

    • Aedesin: structure and antimicrobial activity against multidrugresistant bacterial strains.