• DRAMP ID

    • DRAMP00856
    • Peptide Name

    • Kalata-B1 (Plant defensin)
    • Source

    • Oldenlandia affinis
    • Family

    • Belongs to the cyclotide family
    • Gene

    • OAK1
    • Sequence

    • GLPVCGETCVGGTCNTPGCTCSWPVCTRN
    • Sequence Length

    • 29
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral
    • Target Organism

      • [Ref.10430870]Gram-positive bacterium: Staphylococcus aureus (MIC=0.26 µM), Micrococcus luteus (MIC=40.4 µM);
      • Gram-negative bacterium: Klebsiella oxytoca (MIC=54.8 µM);
      • Fungi: Candida kefyr (MIC=21.4 µM).
      • [Ref.18008336]Virus:HIV:inhibition the cytopathic effects of HIV-1 infection in cultured human T-lymphoblast (CEM-SS) cells(EC50=140 nM).
    • Hemolytic Activity

      • [Ref.12779323] HD50 = 300 μM against Human type A red blood cells.
    • Cytotoxicity

      • [Ref.18008336]CEM-SS cells:IC50=3500 nM.
    • Binding Target

    • Cell membrance
    • Linear/Cyclic

    • Cyclic
    • N-terminal Modification

    • Cyclization (N termini to C termini)
    • C-terminal Modification

    • Cyclization (C termini to N termini)
    • Nonterminal Modifications and Unusual Amino Acids

    • [Ref.7703226] There are three disulfide bonds between Cys5 and Cys19, Cys9 and Cys21, Cys14 and Cys26.
    • Stereochemistry

    • L
    • Structure

    • Beta strand (3 strands; 7 residues)
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP00856 helical wheel diagram
    • PDB ID

    • 2KHB resolved by NMR.
  • 2KHB-> 
    • Predicted Structure

    • There is no predicted structure for DRAMP00856.
    • Formula

    • C117H187N35O40S6
    • Absent Amino Acids

    • ADFHIKMQY
    • Common Amino Acids

    • C
    • Mass

    • 2916.34
    • PI

    • 5.96
    • Basic Residues

    • 1
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 5
    • Net Charge

    • 0
    • Boman Index

    • -19.51
    • Hydrophobicity

    • 0.152
    • Aliphatic Index

    • 43.45
    • Half Life

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

    • 5875
    • Absorbance 280nm

    • 209.82
    • Polar Residues

    • 19

DRAMP00856

DRAMP00856 chydropathy plot
    • Function

    • Probably participates in a plant defense mechanism. Has antibiotic activity. Has a diuretic effect. Has a uterotonic effect in humans. Active against the Gram-positive S. aureus. Relatively ineffective against Gram-negative bacteria such as E. coli and P. aeruginosa. Inhibitory effect on the growth and development of larvae from H. punctigera. The unmodified form has hemolytic activity, the oxidized form lacks hemolytic activity. If the protein is linearized, hemolytic activity is lost.
    • MOA

    • a small number of cyclotides bind to the membrane surface and then insert first into the outer membrane leaflet followed by penetration through the membrane and pore formation. At higher concentrations of cyclotides, destabilization of membranes occurs.
    • Tissue specificity

    • Leaves and stems. Lower in roots.
    • Pharmaceutical use

    • The uteroactive properties of Kalata have been discovered by African traditional medicine. It is used as an ingredient of a herbal tea to accelerate childbirth.
    • PTM

    • Kalata-B1 is a cyclic peptide which contains three disulfide bonds 5-19; 11-21; 14-26.
  • ·Literature 1
    • Title

    • Cyclotides as natural anti-HIV agents.
    • Reference

    • Biopolymers. 2008;90(1):51-60.
    • Author

    • Ireland DC, Wang CK, Wilson JA, Gustafson KR, Craik DJ.
  • ·Literature 2
    • Title

    • An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides.
    • Reference

    • Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8913-8918.
    • Author

    • Tam JP, Lu YA, Yang JL, Chiu KW.
  • ·Literature 3
    • Title

    • Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1.
    • Reference

    • Biochemistry. 1995 Apr 4;34(13):4147-4158.
    • Author

    • Saether O, Craik DJ, Campbell ID, Sletten K, Juul J, Norman DG.
  • ·Literature 4
    • Title

    • The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides.
    • Reference

    • Chembiochem. 2007 Jun 18;8(9):1001-1011.
    • Author

    • Plan MR, Göransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ.
  • ·Literature 5
    • Title

    • Cyclotides insert into lipid bilayers to form membrane pores and destabilize the membrane through hydrophobic and phosphoethanolamine-specific interactions.
    • Reference

    • J Biol Chem. 2012 Dec 21;287(52):43884-98.
    • Author

    • Wang CK, Wacklin HP, Craik DJ.