• DRAMP ID

    • DRAMP29046
    • Peptide Name

    • PAMP(9-20) ( the C-terminal 12-residues of PAMP)
    • Source

    • Homo sapiens et.al
    • Family

    • Belongs to the adrenomedullin family
    • Gene

    • ADM
    • Sequence

    • FRKKWNKWALSR
    • Sequence Length

    • 12
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-
    • Target Organism

      • [Ref.32439180] Gram-negative bacteria: E. coli (MIC = 4 μM), P. aeruginosa (MIC = 16 μM), S. typhimurium (MIC = 4 μM)
      • Gram-positive bacteria:B. subtilis (MIC = 8 μM), S. epidermidis (MIC = 8 μM), S. aureus(MIC = 16 μM)
    • Hemolytic Activity

      • [Ref.32439180]HC10 > 256 μM against sheep RBCs.Note: HC10 is the minimum peptide concentration that caused >10% hemolysis of sheep red blood cells.
    • Cytotoxicity

      • Not found
    • Binding Target

    • Bacterial DNA
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Amidation
    • Nonterminal Modifications and Unusual Amino Acids

    • None
    • Stereochemistry

    • L
    • Structure

    • α-helical (most likely)
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP29046 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP29046.
    • Formula

    • C77H118N24O15
    • Absent Amino Acids

    • CDEGHIMPQTVY
    • Common Amino Acids

    • K
    • Mass

    • 1619.94
    • PI

    • 12.02
    • Basic Residues

    • 5
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 5
    • Net Charge

    • +5
    • Boman Index

    • -4216
    • Hydrophobicity

    • -1.533
    • Aliphatic Index

    • 40.83
    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 11000
    • Absorbance 280nm

    • 1000
    • Polar Residues

    • 2

DRAMP29046

    • Function

    • Kuwasako et al. identified the C-terminal 12-residues of PAMP [PAMP(9–20)] in porcine adrenal medulla as a major endogenous active peptide of the AM precursor and demonstrated that its hypotensive activity is comparable to that of PAMP. PAMP(9-20) can acts as an potent antimicrobial peptide which is more selective than melittin, and antimicrobial action of PAMP(9-20) seems to exert via an intracellular target.
  • ·Literature 1
    • Title

    • Proadrenomedullin N-terminal 20 peptide (PAMP) and its C-terminal 12-residue peptide, PAMP(9-20): Cell selectivity and antimicrobial mechanism
    • Reference

    • Biochem Biophys Res Commun. 2020 Jun 30;527(3):744-750. doi: 10.1016/j.bbrc.2020.04.063. Epub 2020 May 18.
    • Author

    • Ajish C, Yang S, Kumar SD, Shin SY.