General Information

    • DRAMP ID

    • DRAMP03826

    • Peptide Name

    • Ovispirin-1 (OV-1; N-terminal 18 amino acids of SMAP-29)

    • Source

    • Synthetic construct

    • Family

    • Not found

    • Gene

    • Not found

    • Sequence

    • KNLRRIIRKIIHIIKKYG

    • 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=0.7-5.6 µg/ml), Stenotrophomonas maltophilia 5 strains (MIC=0.5-2.2 µg/ml);
      • Gram-positive bacteria: Listeria monocytogenes EGD [n=3] (MIC=1.5±0.3 µg/ml), Staphylococcus aureus 930918 [n=3] (MIC=1.0±0.13 µg/ml).

    • Hemolytic Activity

      • [Ref.11932493]55% hemolytic at 40 µg/mL, 70.2% 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 (1 helices; 13 residues)

    • Structure Description

    • Ovispirin-1 is a uniform α-helix over residues 4-16.

    • Helical Wheel Diagram

    • DRAMP03826 helical wheel diagram

    • PDB ID

    • 1HU5 resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP03826.

Physicochemical Information

    • Formula

    • C105H188N34O21

    • Absent Amino Acids

    • ACDEFMPQSTVW

    • Common Amino Acids

    • I

    • Mass

    • 2262.86

    • PI

    • 11.75

    • Basic Residues

    • 8

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 7

    • Net Charge

    • +8

    • Boman Index

    • -43.02

    • Hydrophobicity

    • -0.372

    • Aliphatic Index

    • 151.67

    • Half Life

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

    • Extinction Coefficient Cystines

    • 1490

    • Absorbance 280nm

    • 87.65

    • Polar Residues

    • 3

DRAMP03826

DRAMP03826 chydropathy plot

Comments Information

    • Function

    • Possess potently antimicrobial activity. It is also highly cytotoxic to human epithelial cells (ME-180 cervical cells

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.