General Information

    • 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

Activity Information

    • 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

Structure Information

    • 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

    • There is no predicted structure for DRAMP03405.

Physicochemical Information

    • 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

Comments Information

    • 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 Information

  • ·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.