General Information

    • DRAMP ID

    • DRAMP02270

    • Peptide Name

    • Magainin-1 (Magainin I; chain of Magainins; Frogs, amphibians, animals)

    • Source

    • Xenopus laevis (African clawed frog)

    • Family

    • Belongs to the magainin family

    • Gene

    • magainins

    • Sequence

    • GIGKFLHSAGKFGKAFVGEIMKS

    • Sequence Length

    • 23

    • Protein Existence

    • Protein level

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

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP02270 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP02270.

Physicochemical Information

    • Formula

    • C112H177N29O28S

    • Absent Amino Acids

    • CDNPQRTWY

    • Common Amino Acids

    • G

    • Mass

    • 2409.87

    • PI

    • 10

    • Basic Residues

    • 5

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 9

    • Net Charge

    • +4

    • Boman Index

    • -2.06

    • Hydrophobicity

    • 0.217

    • Aliphatic Index

    • 72.17

    • Half Life

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

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 7

DRAMP02270

DRAMP02270 chydropathy plot

Comments Information

    • 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 Information

  • ·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.

    • Reference

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

    • Author

    • Zasloff M.