General Information

    • DRAMP ID

    • DRAMP21497

    • Peptide Name

    • MEP-Ns-3

    • Sequence

    • GFLSⓍLKKⓍLPKⓍJAHⓍK

    • Sequence Length

    • 18

    • Original Sequence

    • GFLSILKKVLPKVMAHMK

    • Source

    • Synthetic construct

    • SMILES

    • O=C(NC(C(=O)NC1(C)C(=O)NC(CC(C)C)C(=O)NC(CCCC[NH3+])C(=O)NC(CCCC[NH3+])C(=O)NC(C(=O)NC(C(=O)N2C(C(=O)NC(C(=O)NC3(C)C(=O)NC(CCCC)C(=O)NC(C)C(=O)NC(Cc4nc[nH]c4)C(=O)NC(C(=O)NC(C=O)CCCC[NH3+])(C)CCCC=CCCC3)CCCC[NH3+])CCC2)CC(C)C)(C)CCCC=CCCC1)CO)C(NC(=O)C(NC(=O)C[NH3+])Cc1ccccc1)CC(C)C

Activity Information

    • Biological Activity

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

    • Comments

    • Function: Antibacterial activity against Gram-positive and Gram-negative bacteria. Antifungal activity against Candida albicans is not noteable under 100 μM.

    • Target Organism

      • [Ref.22526241] Gram-positive bacteria: Micrococcus luteus (MIC = 1.3 μM), Bacillus subtilis (MIC = 1.2 μM), Staphylococcus aureus (MIC ≥ 100 μM);
      • Gram-negative bacteria: E.coli (MIC = 46.7 μM), Pseudomonas aeruginosa (MIC > 100 μM);
      • Fungi: Candida albicans (MIC > 100 μM).

    • Hemolytic Activity

      • [Ref.22526241] LC50 = 13.9 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. ②Ⓧ (position: 5, 9, 13 and 17) are 2-(4'-pentenyl) alanine in the S configuration. ③Ⓧ (5) and Ⓧ (9), Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling respectively.

    • Stereochemistry

    • L

    • Secondary Structure

    • ①34% α-helical content in water.②56% α-helical content in 50% TFE. ③48% α-helical content in 8mM SDS.

    • Structure Description

    • On the other hand, the difference in α-helical content between doubly stapled analogs (LL-IIIs-4, MEP-Ns-3, MEP-Ns-5, and MEP-Ns-6) and their unstapled precursors is apparently higher, on average by 15 %
  • There is no predicted structure for DRAMP21497.

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 30.

    • Author

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