General Information

    • DRAMP ID

    • DRAMP03827

    • Peptide Name

    • Novispirin G-10 (mutation of Ovispirin-1)

    • Source

    • Synthetic construct

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • KNLRRIIRKGIHIIKKYG

    • Sequence Length

    • 18

    • UniProt Entry

    • No entry found

    • Protein Existence

    • Synthetic

Activity Information

    • Biological Activity

    • Antibacterial, Cytotoxic, Anti-Gram+, Anti-Gram-, Antimicrobial

    • Target Organism

      • [Ref.11932493]Gram-negative bacteria: Pseudomonas aeruginosa 9 strains (MIC=0.11-12.7 µg/ml), Stenotrophomonas maltophilia 5 strains (MIC=0.29-3.6 µg/ml);
      • Gram-positive bacteria: Listeria monocytogenes EGD [n=3] (MIC=1.4±0.4 µg/ml), Staphylococcus aureus 930918 [n=3] (MIC=4.6±1.7 µg/ml).

    • Hemolytic Activity

      • [Ref.11932493]1.8% hemolytic at 40 µg/mL, 2.5% hemolytic activity at 80 µg/mL against human red blood cells

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Free

    • Nonterminal Modifications and Unusual Amino Acids

    • Free

    • Stereochemistry

    • L

    • Structure

    • Alpha helix (2 helices; 11 residues)

    • Structure Description

    • Novispirin G-10 shows an α-helix-hinge-310 helix structural motif with residues 4-11 forming the α-helix, residues 12 and 13 forming the hinge and residues 14-16 forming the 310 helix.

    • Helical Wheel Diagram

    • DRAMP03827 helical wheel diagram

    • PDB ID

    • 1HU6 resolved by NMR.
  • 1HU6-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP03827.

Physicochemical Information

    • Formula

    • C101H180N34O21

    • Absent Amino Acids

    • ACDEFMPQSTVW

    • Common Amino Acids

    • I

    • Mass

    • 2206.76

    • PI

    • 11.75

    • Basic Residues

    • 8

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 6

    • Net Charge

    • +8

    • Boman Index

    • -47

    • Hydrophobicity

    • -0.644

    • Aliphatic Index

    • 130

    • Half Life

      • Mammalian:1.3 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 1490

    • Absorbance 280nm

    • 87.65

    • Polar Residues

    • 4

DRAMP03827

DRAMP03827 chydropathy plot

Comments Information

    • Function

    • Possess potently antimicrobial activity. Also has hemolytic activity against Human red blood cells, and has cytotoxicity activity against ME-180 cervical cells (33.2% at 200 µg/ml, 5.0% at 50 µg/ml, 7.1% at 25 µg/ml) and A-549 pulmonary cells (33.2% at 200 µg/ml, 14.6% at 50 µg/ml, 10.0% at 25 µg/ml).

Literature Information

  • ·Literature 1

    • Title

    • Impact of single-residue mutations on the structure and Function: of ovispirin/novispirin antimicrobial peptides.

    • Reference

    • Protein Eng. 2002 Mar;15(3):225-232.

    • Author

    • Sawai MV, Waring AJ, Kearney WR, McCray PB Jr, Forsyth WR, Lehrer RI, Tack BF.