General Information

    • DRAMP ID

    • DRAMP21628

    • Peptide Name

    • E2EM15W-S1

    • Sequence

    • TLKQFⓍKGVⓍKWLVK

    • Sequence Length

    • 15

    • Original Sequence

    • TLKQFAKGVGKWLVK

    • Source

    • Synthetic construct

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+

    • Comments

    • Function: Antibcaterial activity against Gram-positive bacteria. Antibacterial activity against Gram-negative bacteria is not noteable under 200 μg/mL.

    • Target Organism

      • [Ref.24211019] Gram-positive bacteria: Bacillus subtilis (MIC = 3.13 μg/mL), Staphylococcus aureus (MIC = 3.13 μg/mL), Staphylococcus epidermis (MIC > 200 μg/mL);
      • Gram-negative bacteria: Escherichia coli (MIC > 200 μg/mL), Shigella dysentariae (MIC > 200 μg/mL), Salmonella typhimurium (MIC > 200 μg/mL), Klebsiella pneumonia (MIC > 200 μg/mL), Proteus mirabilis (MIC > 200 μg/mL), Pseudomonas aeuginose (MIC > 200 μg/mL).

    • Hemolytic Activity

      • [Ref.24211019] No hemolytic activity information found.

    • Cytotoxicity

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

Structure Information

    • Linear/Cyclic

    • Cyclic (Stapled)

    • N-terminal Modification

    • Acetylation

    • C-terminal Modification

    • Amidation

    • Special Amino Acid and Stapling Position

    • ①The Ⓧ (position: 6 and 10) in sequence indicates (S)-α-methyl, α-pentenylglycine. ②Ⓧ (6) and Ⓧ (10) are cross-linked by hydrocarbon stapling through an oct-4-enyl staple.

    • Stereochemistry

    • L

    • Secondary Structure

    • 47% α-helical content in a 25 mM potassium phosphate buffer solution at 20 ℃.

    • Structure Description

    • ①On the other hand, all three stapled analogs of E2EM15W showed substantial increases in helical contents, which again demonstrated the highly effective helix-stabilization through the all-hydrocarbon stapling technology. ②E2EM15W-S1, the most potent analog in the antimicrobial assay, showed the highest degree of helicity (47%) in the aqueous solution, supporting a close correlation between the helicity and the antimicrobial activity of the peptides in this series.

    • Helical Wheel Diagram

    • DRAMP21628 helical wheel diagram

    • Predicted Structure

Literature Information

  • Literature 1

    • Title

    • Truncated and constrained helical analogs of antimicrobial esculentin-2EM

    • Reference

    • Bioorg Med Chem Lett. 2013 Dec 15;23(24):6717-20. doi: 10.1016/j.bmcl.2013.10.031. Epub 2013 Oct 26.

    • Author

    • Thanh Kim Pham, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim