General Information

    • DRAMP ID

    • DRAMP21495

    • Peptide Name

    • MEP-Ns-1

    • Sequence

    • GFLSILKKVLPKⓍJAHⓍK

    • Sequence Length

    • 18

    • Original Sequence

    • GFLSILKKVLPKVMAHMK

    • Source

    • Synthetic construct

Activity Information

    • Biological Activity

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

    • Comments

    • Function: Antibacterial activity against Gram-positive and Gram-negative bacteria and Antifungal activity against Candida albicans.

    • Target Organism

      • [Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 0.8 μM), Bacillus subtilis (MIC = 1.1 μM), Staphylococcus aureus (MIC = 10.8 μM);
      • Gram-negative bacteria: E.coli (MIC = 2.5 μM), Pseudomonas aeruginosa (MIC = 77 μM);
      • Fungi: Candida albicans (MIC = 30 μM).

    • Hemolytic Activity

      • [Ref.22526241] LC50 = 18.1 μM. Note: LC50 is the concentration of a peptide able to lyse 50% of human erthrocytes in the assay.

    • Cytotoxicity

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

Structure Information

    • Linear/Cyclic

    • Cyclic (Stapled)

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Special Amino Acid and Stapling Position

    • ①The J (position: 14) in sequence indicates norleucine. ②The Ⓧ (position: 13 and 17) indicates 2-(4'-pentenyl) alanine in the S configuration. ③Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling.

    • Stereochemistry

    • L

    • Secondary Structure

    • ①19% α-helical content in water.②66% α-helical content in 50% TFE. ③75% α-helical content in 8mM SDS.

    • Structure Description

    • The CD spectra of the singly stapled peptides of the i, i + 4 type acquired in water show a slight increase (by 5 %) of helical content in the case of MEP-Ns-1, MEP-Ns-2 and LL-IIIs-3 compared to their unstapled precursors.

    • Helical Wheel Diagram

    • DRAMP21495 helical wheel diagram

    • Predicted Structure

    • There is no predicted structure for DRAMP21495.

Literature Information

  • Literature 1

    • Title

    • Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera

    • Reference

    • Amino Acids. 2012 Nov;43(5):2047-58. doi: 10.1007/s00726-012-1283-1. Epub 2012 Apr 28.

    • Author

    • Hubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský