General Information

    • DRAMP ID

    • DRAMP00387

    • Peptide Name

    • Antimicrobial peptide 1 (EcAMP1; hairpin-like peptides; Plants)

    • Source

    • Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli)

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • GSGRGSCRSQCMRRHEDEPWRVQECVSQCRRRRGGGD

    • Sequence Length

    • 37

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antifungal

    • Target Organism

      • Fungi: Alternaria alternata (EC50=16.0±2.3 µM), A. solani (EC50=14.0±2.1 µM), Aspergillus niger (EC50>32 µM), Bipolaris sorokiniana (EC50=18.2±2.7 µM), Colletotrichum graminicola (EC50>10 µM), Diplodia maydis (EC50>10 µM), Fusarium graminearum (EC50=4.5±1.4 µM), Fusarium oxysporum (EC50=8.5±1.6 µM), F. solani (EC50=4.0±1.2 µM), F. verticillioides (EC50=8.1±2.3 µM), Phoma betae (EC50=6.0±1.5 µM), Phytophthora infestans (EC50=16.3±2.5 µM), Pythium debaryanum (EC50=12.0±1.7 µM), P. ultimum (EC50=14.4±2.1 µM), Tritirachium album (EC50>32 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

    • 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 (3 helices; 20 residues)

    • Structure Description

    • The peptide adopts a disulfide-stabilized alpha-helical hairpin structure in aqueous solution and thus represents a novel fold among naturally occurring antimicrobial peptides.

    • Helical Wheel Diagram

    • DRAMP00387 helical wheel diagram

    • PDB ID

    • 2L2R resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP00387.

Physicochemical Information

    • Formula

    • C165H274N70O55S5

    • Absent Amino Acids

    • AFIKLNTY

    • Common Amino Acids

    • R

    • Mass

    • 4278.73

    • PI

    • 9.47

    • Basic Residues

    • 10

    • Acidic Residues

    • 5

    • Hydrophobic Residues

    • 3

    • Net Charge

    • +5

    • Boman Index

    • -183.51

    • Hydrophobicity

    • -1.608

    • Aliphatic Index

    • 15.68

    • Half Life

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

    • Extinction Coefficient Cystines

    • 5750

    • Absorbance 280nm

    • 159.72

    • Polar Residues

    • 14

DRAMP00387

DRAMP00387 chydropathy plot

Comments Information

    • Function

    • EcAMP1 can inhibit growth of several fungal phytopathogens. Does not destroy spores but rather inhibits hyphal growth during germination. Does not affect spore germination in A. niger, C. graminicola, D. maydis and T. album. Does not inhibit trypsin. Confocal microscopy revealed intensive EcAMP1 binding to the surface of fungal conidia followed by internalization and accumulation in the cytoplasm without disturbance of membrane integrity.

    • Tissue specificity

    • Seed.

Literature Information

  • ·Literature 1

    • Title

    • Defense peptides from barnyard grass (Echinochloa crusgalli L.) seeds.

    • Reference

    • Peptides. 2012 Nov;38(1):33-40.

    • Author

    • Rogozhin EA, Ryazantsev DY, Grishin EV, Egorov TA, Zavriev SK.
  • ·Literature 2

    • Title

    • Disulfide-stabilized helical hairpin structure and activity of a novel antifungal peptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli).

    • Reference

    • J Biol Chem. 2011 Jul 15;286(28):25145-25153.

    • Author

    • Nolde SB, Vassilevski AA, Rogozhin EA, Barinov NA, Balashova TA, Samsonova OV, Baranov YV, Feofanov AV, Egorov TA, Arseniev AS, Grishin EV.