• • DRAMP ID

  • DRAMP03173

• • Peptide Name

  • Arenicin-1 (Ar-1; marine polychaeta, animals)

• • Source

  • Arenicola marina (Lugworm) (Lumbricus marinus)

• • Family

  • Not found

• • Gene

  • Not found

• • Sequence

  • RWCVYAYVRVRGVLVRYRRCW

• • Sequence Length

  • 21

• • UniProt Entry

  • Q5SC60,P84105

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • Target Organism

  • • Gram-positive bacterium: Listeria monocytogenes EGD (MIC=0.6 µg/ml);
    • Gram-negative bacteria: Escherichia coli ML-35p (MIC=4 µg/ml), E. coli WBB01 (MIC=0.3 mM), E. coli ATCC 23716 (MIC=0.6 mM), Salmonella enterica R595 (MIC=0.3 mM), S. enterica R60 (MIC=1.25 mM), Proteus mirabilis R45 (MIC=0.6 mM).
    • Yeast: Candida albicans 820 (MIC=20 µg/ml).
    • Human Jurkat T-cells: LD50>40 mM (35.5% lysis at 30 mM).

• • Hemolytic Activity

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

• • Cytotoxicity

  • • [Ref.27940358] Cytotoxicity: human embryonic fibroblasts (HEF) and human red blood cells (hRBC)(IC50 for arenicin-1 in the presence or absence of 10% FBS were of 35 and 8 μM,HC50 indicating 50% hemolysis after 24 h incubation, equaled to 16μM).

• • 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

  • Arenicin-1 is a two-stranded antiparallel β-sheet (Cys3-Val10 and Val13-Cys20) stabilized by nine intra-backbone hydrogen bonds and a disulfide bond between Cys3 and Cys20. The strands of the β-sheet are connected by a type I´ β-turn. The surface of arenicin is amphiphilic, with distinct hydrophobic and hydrophilic areas (ref.2).

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 2JSB resolved by NMR.
• 2JSB-> 

• Predicted Structure

• Please click DRAMP03173_predicted_structure.pdb to download.

DRAMP03173

• • 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.