• • DRAMP ID

  • DRAMP03174

• • Peptide Name

  • Arenicin-2 (Ar-2; marine polychaeta, animals)

• • Source

  • Arenicola marina (Lugworm) (Lumbricus marinus)

• • Family

  • Not found

• • Gene

  • Not found

• • Sequence

  • RWCVYAYVRIRGVLVRYRRCW

• • Sequence Length

  • 21

• • UniProt Entry

  • Q5SC59,P84106

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • Target Organism

  • • Gram-positive bacterium: Listeria monocytogenes EGD;
    • Gram-negative bacterium: Escherichia coli ML-35p.
    • Yeast: Candida albicans 820.

• • 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

  • Anionic lipid vesicles

• • Linear/Cyclic

  • Cyclic

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Free

• • Nonterminal Modifications and Unusual Amino Acids

  • Disulfide bond between Cys3 and Cys20.

• • Stereochemistry

  • L

• • Structure

  • Beta strand (2 strands; 16 residues)

• • Structure Description

  • NMR investigation shows that in water solution arenicin-2 displays a prolonged beta-hairpin, formed by two antiparallel beta-strands and stabilized by one disulfide and nine hydrogen bonds. A significant right-handed twist in the beta-sheet is deprived the peptide surface of amphipathicity. CD spectroscopic analysis indicates that arenicin-2 binds to the SDS and DPC micelles, and conformation of the peptide is significantly changed upon

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 2JNI,2L8X resolved by NMR.
• 2JNI-> 

• Predicted Structure

• There is no predicted structure for DRAMP03174.

DRAMP03174

• • Function

  • Has antimicrobial activity against the Gram-negative bacteria, Gram-positive bacteriua as well as yeast C. albicans. Bacterial killing occurs within minutes and is accompanied by membrane permeabilization, membrane detachment and release of cytoplasm. Interaction of arenicin with reconstituted membranes that mimic the lipopolysaccharide-containing outer membrane or the phospholipid-containing plasma membrane of Gram-negative bacteria exhibited no pronounced lipid specificity.

• • PTM

  • Contains one disulfide bond 3-20.

• • Domian

  • Contains 1 BRICHOS domain.

• ·Literature 1

• • Title

  • Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina.

• • Pubmed ID

  • 15527787

• • Reference

  • FEBS Lett. 2004 Nov 5;577(1-2):209-214.

• • Author

  • Ovchinnikova TV, Aleshina GM, Balandin SV, Krasnosdembskaya AD, Markelov ML, Frolova EI, Leonova YF, Tagaev AA, Krasnodembsky EG, Kokryakov VN.

• ·Literature 2

• • Title

  • Structure and mode of action of the antimicrobial peptide arenicin.

• • Pubmed ID

  • 17935487

• • Reference

  • Biochem J. 2008 Feb 15;410(1):113-122.

• • Author

  • Andrä J, Jakovkin I, Grötzinger J, Hecht O, Krasnosdembskaya AD, Goldmann T, Gutsmann T, Leippe M.

• ·Literature 3

• • Title

  • Recombinant expression, synthesis, purification, and solution structure of arenicin.

• • Pubmed ID

  • 17585874

• • Reference

  • Biochem Biophys Res Commun. 2007 Aug 17;360(1):156-162.

• • Author

  • Ovchinnikova TV, Shenkarev ZO, Nadezhdin KD, Balandin SV, Zhmak MN, Kudelina IA, Finkina EI, Kokryakov VN, Arseniev AS.