• • 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

• • UniProt Entry

  • P86698

• • Protein Existence

  • Protein level

• • SMILES

  • Not available

• • Biological Activity

  • Antimicrobial, Antifungal

• • Target Organism

  • • Fungi:

      Target Organism	Activity
      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

• • 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.

• • PDB ID

  • 2L2R resolved by NMR.

• Predicted Structure

• There is no predicted structure for DRAMP00387.

DRAMP00387

• • 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 1

• • Title

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

• • Pubmed ID

  • 22940285

• • 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).

• • Pubmed ID

  • 21561864

• • 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.