General Information

    • DRAMP ID

    • DRAMP00977

    • Peptide Name

    • Antimicrobial peptide 2 (AC-AMP2; Plant defensin)

    • Source

    • Amaranthus caudatus (Love-lies-bleeding) (Inca-wheat)

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • VGECVRGRCPSGMCCSQFGYCGKGPKYCGR

    • Sequence Length

    • 30

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Antifungal

    • Target Organism

      • Gram-positive bacteria: Bacillus megaterium (IC50=40 µg/ml), Sarcina lutea (IC50=250 µg/ml).
      • Fungi: Alternaria brassicola (IC50=7 µg/ml), Ascochyta pisi (IC50=8 µg/ml), Botrytis cinera (IC50=10 µg/ml), Colletotrichum lindemuthianum (IC50=8 µg/ml), Fusarium culmorum (IC50=2 µg/ml), Trichoderma hamatum (IC50=7 µg/ml), Verticillium dahliae (IC50=6 µg/ml).

    • Hemolytic Activity

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

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Chitin-binding

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

    • Beta strand

    • Structure Description

    • The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified.

    • Helical Wheel Diagram

    • DRAMP00977 helical wheel diagram
  • 1MMC-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP00977.

Physicochemical Information

    • Formula

    • C130H206N42O38S7

    • Absent Amino Acids

    • ADHILNTW

    • Common Amino Acids

    • G

    • Mass

    • 3189.74

    • PI

    • 8.92

    • Basic Residues

    • 5

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 3

    • Net Charge

    • +4

    • Boman Index

    • -47.62

    • Hydrophobicity

    • -0.347

    • Aliphatic Index

    • 19.33

    • Half Life

      • Mammalian:100 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 3355

    • Absorbance 280nm

    • 115.69

    • Polar Residues

    • 17

DRAMP00977

DRAMP00977 chydropathy plot

Comments Information

    • Function

    • Chitin-binding protein with a defensive Function

    • Miscellaneous

    • Its chitin-binding activity is strongly inhibited by divalent cations.

    • PTM

    • Contains three disulfide bonds 4-15; 9-21; 14-28.

Literature Information

  • ·Literature 1

    • Title

    • Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins.

    • Reference

    • Biochemistry. 1992 May 5;31(17):4308-4314.

    • Author

    • Broekaert W.F, Marien W, Terras F.R.G, de Bolle M.F.C, Proost P, van Damme J, Dillen L, Claeys M, Rees S.B, Vanderleyden J, Cammue B.P.A.
  • ·Literature 2

    • Title

    • H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.

    • Reference

    • J Mol Biol. 1996 May 3;258(2):322-333.

    • Author

    • Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P.
  • ·Literature 3

    • Title

    • Reference

    • J Pept Res. 1997 Apr;49(4):336-340.

    • Author

    • el Bouyoussfi M, Laus G, Verhey