General Information

    • 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

    • SMILES

    • CC(C)C[C@H](NC(=O)[C@H](C)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](N)Cc1ccccc1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(=N)N)C(N)=O

Activity Information

    • Biological Activity

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

    • Target Organism

      • [Ref.32439180] Gram-negative bacteria:
        Target OrganismActivity
        E. coliMIC = 4 μM
        P. aeruginosaMIC = 16 μM
        S. typhimuriumMIC = 4 μM
      • Gram-positive bacteria:
        Target OrganismActivity
        B. subtilisMIC = 8 μM
        S. epidermidisMIC = 8 μM
        S. aureusMIC = 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

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • Stereochemistry

    • L

    • Structure

    • α-helical (most likely)

    • Structure Description

    • Not found

    • PDB ID

    • Predicted Structure

    • There is no predicted structure for DRAMP29046.

Physicochemical Information

    • 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

Comments Information

    • 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 Information

  • ·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.