General Information

    • DRAMP ID

    • DRAMP03962

    • Peptide Name

    • Cecropin A(1-8)-Magainin 2(1-12)hybrid peptide (CAMA)

    • Source

    • Synthetic construct

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • KWKLFKKIGIGKFLHSAKKF

    • Sequence Length

    • 20

    • Protein Existence

    • Synthetic

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial

    • Target Organism

    • No MICs found in DRAMP database

    • 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

    • Not included yet

    • N-terminal Modification

    • Not included yet

    • C-terminal Modification

    • Not included yet

    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet

    • Stereochemistry

    • Not included yet

    • Structure

    • Alpha helix

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP03962 helical wheel diagram
  • 1F0D-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP03962.

Physicochemical Information

    • Formula

    • C120H190N30O22

    • Absent Amino Acids

    • CDEMNPQRTVY

    • Common Amino Acids

    • K

    • Mass

    • 2405.02

    • PI

    • 10.78

    • Basic Residues

    • 8

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 9

    • Net Charge

    • +8

    • Boman Index

    • -12.27

    • Hydrophobicity

    • -0.31

    • Aliphatic Index

    • 83

    • Half Life

      • Mammalian:1.3 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 5500

    • Absorbance 280nm

    • 289.47

    • Polar Residues

    • 3

DRAMP03962

DRAMP03962 chydropathy plot

Comments Information

    • MOA

    • The partial insertion of the Trp2 of CA-MA into the membrane, as well as the electrostatic interactions between the positively charged Lys residues at the N-terminus of the CA-MA and the anionic phospholipid headgroups, leads to the primary binding to the cell membrane. Then, the flexibility or bending potential induced by the Gly-Ile-Gly hinge sequence or the Pro residue in the central part of the peptides may allow the alpha-helix in the C-terminus to span the lipid bilayer.

Literature Information

  • ·Literature 1

    • Title

    • Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures.

    • Reference

    • Biochemistry. 2000 Oct 3;39(39):11855-11864.

    • Author

    • Oh D, Shin SY, Lee S, Kang JH, Kim SD, Ryu PD, Hahm KS, Kim Y.