• • DRAMP ID

  • DRAMP02271

• • Peptide Name

  • Magainin-2 (Magainin II; chain of Magainins; Frogs, amphibians, animals)

• • Source

  • Xenopus ruwenzoriensis (Uganda clawed frog)

• • Family

  • Belongs to the gastrin/cholecystokinin family. Magainin subfamily.

• • Gene

  • N/A

• • Sequence

  • GIGKFLHSAKKFGKAFVGEIMNS

• • Sequence Length

  • 23

• • UniProt Entry

  • C0HKN6

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • Target Organism

  • • Gram-negative bacteria: Escherichia coli D31 (MIC=5 µg/ml), Klebsiella pneumoniae (MIC=10 µg/ml), Escherichia coli (MIC=50 µg/ml), Pseudomonas putida (MIC=10 µg/ml), Citrobacter freundii (MIC=30 µg/ml), Enterobacter cloacae (MIC=50 µg/ml), Pseudomonas aeruginosa (MIC=100 µg/ml), Serratia marcescens (MIC=100 µg/ml), Proteus mirabilis (MIC>100 µg/ml);
    • Gram-positive bacteria: Staphylococcus epidermidis (MIC=10 µg/ml), Staphylococcus aureus (MIC=50 µg/ml), Streptococcus fecalis (MIC>100 µg/ml).
    • Protozoa: Paramecium caudatum (MIC=10 µg/ml).
    • Yeast: Candida albicans (MIC=80 µg/ml).

• • 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

  • 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

  • The secondary structure is shown to be helical in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution.

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 2MAG,2LSA resolved by NMR.
• 2MAG-> 

• Predicted Structure

• Please click DRAMP02271_predicted_structure.pdb to download.

DRAMP02271

• • Function

  • Antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. Magainins are membrane lytic agents.

• • Tissue specificity

  • Synthesized in the stomach and stored in a novel granular multinucleated cell in the gastric mucosa. It is stored as active, processed peptides in large granules within the granular gland secretions of the skin.

• ·Literature 1

• • Title

  • Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.

• • Pubmed ID

  • 3299384

• • Reference

  • Proc Natl Acad Sci U S A. 1987 Aug;84(15):5449-5453.

• • Author

  • Zasloff M.

• ·Literature 2

• • Title

  • Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution.

• • Pubmed ID

  • 9090128

• • Reference

  • J Biomol NMR. 1997 Feb;9(2):127-135.

• • Author

  • Gesell J, Zasloff M, Opella SJ.

• ·Literature 3

• • Title

  • All Atom Simulations of the Initial Binding of Magainin and Pleurocidin to Membranes Comprising a Mixture of Anionic and Zwitterionic

• • Pubmed ID

  • PubMed ID is not available

• • Reference

  • To be Published.

• • Author

  • Vermeer LS, Kozlowska J, Lorenz CD, Mason JA.