• • DRAMP ID

  • DRAMP03812

• • Peptide Name

  • Pardaxin P-4 (Pardaxin P1a; Pardaxin Pa4)

• • Source

  • Pardachirus marmoratus (Finless sole) (Achirus marmoratus)

• • Family

  • Belongs to the pardaxin family

• • Gene

  • Not found

• • Sequence

  • GFFALIPKIISSPLFKTLLSAVGSALSSSGGQE

• • Sequence Length

  • 33

• • UniProt Entry

  • P81861

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • Target Organism

  • • [Ref.23598079] Gram-positive bacteria : Micrococcus luteus(MIC=100 mg/L), Staphylococcus aureus(MIC=50 mg/L), Streptococcus pneumoniae(MIC=100 mg/L), Streptococcus agalactiae(MIC=100 mg/L), Staphylococcus sp.(MIC=6.25 mg/L);
    • Gram-negative bacteria : Grouper Vibrio alginolyticus(MIC=50 mg/L), Vibrio harveyi(MIC=50 mg/L), Vibrio vulnificus(MIC=100 mg/L)

• • Hemolytic Activity

  • • [Ref.23598079] 7% hemolysis at 12.5 mg/L , 10% hemolysis at 25 mg/L , 27% hemolysis at 50 mg/L , 55% hemolysis at 100 mg/L , 95% hemolysis at 200 mg/L , 90% hemolysis at 400 mg/L against sheep red blood cells

• • Cytotoxicity

  • • Not included yet

• • Binding Target

  • Cell membrane

• • 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 (2 helices; 15 residues)

• • Structure Description

  • The peptide adopts a bend-helix-bend-helix motif with an angle between the two structure helices of 122 +/- 9 degrees, making this structure substantially different from the one previously determined in organic solvents.

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 1XC0,2KNS resolved by NMR.

• Predicted Structure

• There is no predicted structure for DRAMP03812.

DRAMP03812

• • Function

  • Exhibits unusual shark repellent and surfactant properties. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis.

• • Domain

  • Consists of a C-terminal hydrophilic region and a predominantly hydrophobic remainder. Function

• ·Literature 1

• • Title

  • Membrane composition determines pardaxin's mechanism of lipid bilayer disruption.

• • Pubmed ID

  • 12124282

• • Reference

  • Biophys J. 2002 Aug;83(2):1004-1013.

• • Author

  • Hallock KJ, Lee DK, Omnaas J, Mosberg HI, Ramamoorthy A.

• ·Literature 2

• • Title

  • NMR structure of pardaxin, a pore-forming antimicrobial peptide, in lipopolysaccharide micelles: mechanism of outer membrane permeabilization.

• • Pubmed ID

  • 19959835

• • Reference

  • J Biol Chem. 2010 Feb 5;285(6):3883-3895.

• • Author

  • Bhunia A, Domadia PN, Torres J, Hallock KJ, Ramamoorthy A, Bhattacharjya S.

• ·Literature 3

• • Title

  • Structure and orientation of pardaxin determined by NMR experiments in model membranes.

• • Pubmed ID

  • 15292173

• • Reference

  • J Biol Chem. 2004 Oct 29;279(44):45815-23.

• • Author

  • Porcelli F, Buck B, Lee DK, Hallock KJ, Ramamoorthy A, Veglia G.

• ·Literature 4

• • Title

  • Truncated antimicrobial peptides from marine organisms retain anticancer activity and antibacterial activity against multidrug-resistant Staphylococcus aureus.

• • Pubmed ID

  • 23598079

• • Reference

  • Peptides. 2013 Jun;44:139-48.

• • Author

  • Lin MC, Hui CF, Chen JY, Wu JL