General Information

    • DRAMP ID

    • DRAMP02933

    • Peptide Name

    • Polyphemusin-1 (PM1; crabs, Arthropods, animals)

    • Source

    • Limulus polyphemus (Atlantic horseshoe crab)

    • Family

    • Belongs to the tachyplesin/polyphemusin family

    • Gene

    • Not found

    • Sequence

    • RRWCFRVCYRGFCYRKCR

    • Sequence Length

    • 18

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

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

    • Target Organism

      • Gram-negative bacteria: Escherichia coli UB1005 (MIC=0.5 µg/ml), E. coli DC2 (MIC=1 µg/ml), Salmonella typhimurium (defensin-sensitive) (MIC=0.25 µg/ml), S. typhimurium (MIC=1 µg/ml), Pseudomonas aeruginosa K799 (MIC=2 µg/ml), P. aeruginosa Z61 (MIC=1 µg/ml);
      • Gram-positive bacteria: Staphylococcus aureus SAP0017 (MIC=2 µg/ml), Staphylococcus epidermidis (MIC=1 µg/ml), Enterococcus faecalis (MIC=1 µg/ml).
      • Yeasy: Candida albicans (MIC=4 µg/ml).

    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry

    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Cyclic

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Nonterminal Modifications and Unusual Amino Acids

    • Disulfide bond between Cys4 and Cys17,Cys8 and Cys13.

    • Stereochemistry

    • L

    • Structure

    • Beta strand (2 strands; 4 residues)

    • Structure Description

    • The solution structure of polyphemusin I is determined using (1)H-NMR spectroscopy. Polyphemusin I is found to be an amphipathic, beta-hairpin connected by a type I' beta-turn.

    • Helical Wheel Diagram

    • DRAMP02933 helical wheel diagram

    • PDB ID

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

    • Predicted Structure

Physicochemical Information

    • Formula

    • C108H164N38O21S4

    • Absent Amino Acids

    • ADEHILMNPQST

    • Common Amino Acids

    • R

    • Mass

    • 2458.97

    • PI

    • 10.33

    • Basic Residues

    • 7

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 4

    • Net Charge

    • +7

    • Boman Index

    • -76.96

    • Hydrophobicity

    • -0.833

    • Aliphatic Index

    • 16.11

    • Half Life

      • Mammalian:1 hour
      • Yeast:2 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 8730

    • Absorbance 280nm

    • 513.53

    • Polar Residues

    • 7

DRAMP02933

DRAMP02933 chydropathy plot

Comments Information

    • Function

    • PM1 showes high antimicrobial activity against the Gram-negative, Gram-positive and fungal specimens tested.

    • Tissue specificity

    • Hemocytes.

    • PTM

    • Contains two disulfide bonds 4-17; 8-13 and C-terminal amidation.

Literature Information

  • ·Literature 1

    • Title

    • Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity.

    • Reference

    • J Biochem. 1989 Oct;106(4):663-668.

    • Author

    • Miyata T, Tokunaga F, Yonega T, Yoshikawa K, Iwanaga S, Niwa M, Takao T, Shimonishi Y.
  • ·Literature 2

    • Title

    • Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I.

    • Reference

    • Biochim Biophys Acta. 2004 May 6;1698(2):239-250.

    • Author

    • Powers JP, Rozek A, Hancock RE.