• • DRAMP ID

  • DRAMP18190

• • Peptide Name

  • Pantinin-3 (Non-disulfide-bridged peptide 4.22, NDBP-4.22, Non-disulfide-bridged peptide 5.23, ND

• • Source

  • Pandinus imperator (Emperor scorpion)

• • Family

  • Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Short an

• • Gene

  • Not found

• • Sequence

  • FLSTIWNGIKSLL

• • Sequence Length

  • 13

• • UniProt Entry

  • R4JJN6

• • Protein Existence

  • Homology

• • Biological Activity

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

• • Target Organism

  • • [Ref.23624072]Gram-positive bacteria: S.aureus (MIC=16 μM), B.magaterium (MIC=6 μM), M.luteus (MIC=8 μM ), VRE (MIC=4 μM), MRSA (MIC=12 μM);
    • Gram-negative bacteria: E.coli (MIC=36 μM), P.putida (MIC >87 μM), K.oxytoca (MIC=87 μM), E.cloacae (MIC >87 μM), S.enterica (MIC=84 μM);
    • Fungus: C.tropicalis (MIC=17 μM).

• • Hemolytic Activity

  • • [Ref.23624072]70% hemolytic activity at 16 μM, 100% hemolytic activity at 32 μM, 100% hemolytic activity at 64 μM against human 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

  • Not found

• • Structure Description

  • Not found

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP18190.

DRAMP18190

• • Function

  • Amphipathic peptide that possesses relatively strong activities against Gram-positive bacteria and a fungus, but has very weak antimicrobial activities against Gram-negative bacteria. Also exhibits hemolytic activities against human erythrocytes. Furthermore, this peptide potently inhibits the growth of vancomycin-resistant Enterococcus (VRE) S13, a pathogen that can cause a number of human infections.Forms an alpha-helical membrane channel in the prey.

• ·Literature 1

• • Title

  • Three new antimicrobial peptides from the scorpion Pandinusimperator.

• • Pubmed ID

  • 23624072

• • Reference

  • Peptides 45:28-34(2013)

• • Author

  • Zeng X.C., Zhou L., Shi W., Luo X., Zhang L., Nie Y., Wang J., Wu S.,Cao B., Cao H.

• ·Literature 2

• • Title

  • Scorpion venom peptides with no disulfide bridges: a review.

• • Pubmed ID

  • 24184590

• • Reference

  • Peptides 51:35-45(2014

• • Author

  • Almaaytah A., Albalas Q.