• DRAMP ID

    • DRAMP03405
    • Peptide Name

    • mCRAMP-1 (mouse cathelin-related antimicrobial peptide 1; cathelicidin; Rodents, mammals, animals
    • Source

    • Mus musculus (Mouse)
    • Family

    • Not found
    • Gene

    • Camp
    • Sequence

    • GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPE
    • Sequence Length

    • 33
    • Protein Existence

    • Transcript level
    • Biological Activity

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

      • Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC=1 µM), Escherichia coli ML35 (MIC=2 µM), Escherichia coli D21 (MIC=8 µM), Pseudomonas aeruginosa ATCC 27853 (MIC=4 µM), Serratia marcescens ATCC 8100 (MIC=4 µM);
      • Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (MIC=32 µM), Staphylococcus aureus Cowan I (MIC=32 µM), Staphylococcus aureus (MRSA) (MIC>64 µM), Staphylococcus aureus (MRSA) (MIC=64 µM), Staphylococcus epidermidis ATCC 12228 (MIC=16 µM), Streptococcus faecalis ATCC 29212 (MIC=16 µM), Bacillus megaterium Bm11 (MIC=4 µM).
      • Fungi: Candida albicans (MIC>64 µM), Cryptococcus neoformans (MIC=16 µM).
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • Free
    • Stereochemistry

    • L
    • Structure

    • Alpha helix (CD)
    • Structure Description

    • The spectra of 10-25 µm synthetic CRAMP-1 in buffer suggest that the peptide is in a random coil configuration and that it will assume a helical structure in the presence of 15–45% (v/v) trifluoroethanol.
    • Helical Wheel Diagram

    • DRAMP03405 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • Formula

    • C173H294N48O44
    • Absent Amino Acids

    • ACDHMSTWY
    • Common Amino Acids

    • K
    • Mass

    • 3750.53
    • PI

    • 10.22
    • Basic Residues

    • 9
    • Acidic Residues

    • 3
    • Hydrophobic Residues

    • 10
    • Net Charge

    • +6
    • Boman Index

    • -53.87
    • Hydrophobicity

    • -0.815
    • Aliphatic Index

    • 91.52
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 6

DRAMP03405

DRAMP03405 chydropathy plot
    • Function

    • Acts as a potent antimicrobial peptide.
    • Tissue specificity

    • Expressed in testis, spleen, stomach, and intestine. Very low expression found in heart, lung and skeletal muscle. No expression in brain, kidney or liver.
  • ·Literature 1
    • Title

    • Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse.
    • Reference

    • J Biol Chem. 1997 May 16;272(20):13088-13093.
    • Author

    • Gallo RL, Kim KJ, Bernfield M, Kozak CA, Zanetti M, Merluzzi L, Gennaro R.
  • ·Literature 2
    • Title

    • A novel murine cathelin-like protein expressed in bone marrow.
    • Reference

    • FEBS Lett. 1996 Aug 5;391(1-2):5-8.
    • Author

    • Popsueva AE, Zinovjeva MV, Visser JW, Zijlmans JM, Fibbe WE, Belyavsky AV.