General Information

    • DRAMP ID

    • DRAMP21494

    • Peptide Name

    • MEP-N

    • Source

    • Synthetic construct

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • GFLSILKKVLPKVJAHJK

    • Sequence Length

    • 18

    • UniProt Entry

    • No entry found

    • Protein Existence

    • Synthetic form

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal

    • Target Organism

      • [Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 1 μM), Bacillus subtilis (MIC = 0.5 μM), Staphylococcus aureus (MIC = 2.5 μM);
      • Gram-negative bacteria: E.coli (MIC = 0.9 μM), Pseudomonas aeruginosa (MIC = 17.3 μM);
      • Fungi: Candida albicans (MIC = 15 μM).

    • Hemolytic Activity

      • [Ref.22526241] LC50 = 50 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.

    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • The J (position: 14 and 17) in sequence are norleucine.

    • Stereochemistry

    • L

    • Structure

    • ①12% α-helical content in water.②43% α-helical content in 50% TFE. ③48% α-helical content in 8mM SDS.

    • Structure Description

    • No other descriptive information about the structure found in the literature

    • Helical Wheel Diagram

    • DRAMP21494 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP21494.

Physicochemical Information

    • Formula

    • C₉₈H₁₇₀N₂₄O₂₀

    • Absent Amino Acids

    • CDEMNQRTWY

    • Common Amino Acids

    • K

    • Mass

    • 2004.58

    • PI

    • 10.48

    • Basic Residues

    • 5

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 0

    • Net Charge

    • +5

    • Boman Index

    • 0

    • Hydrophobicity

    • 0

    • Aliphatic Index

    • 0

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 2

DRAMP21494

DRAMP21494 chydropathy plot

Comments Information

    • Function

    • Antibacterial activity against Gram-positive and Gram-negative bacteria and Antifungal activity against Candida albicans.

Literature Information

  • ·Literature 1

    • Title

    • Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera

    • Reference

    • Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 27.

    • Author

    • Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský