General Information

    • DRAMP ID

    • DRAMP21613

    • Peptide Name

    • S5

    • Sequence

    • KⓍWAKⓍA

    • Sequence Length

    • 7

    • Original Sequence

    • KXWAKXA

    • Source

    • Synthetic construct

Activity Information

    • Biological Activity

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

    • Comments

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

    • Target Organism

      • Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 50 μM), Staphylococcus aureus ATCC 6538p (MIC = 50 μM), Staphylococcus epidermis ATCC 12228 (MIC > 100 μM);
      • Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 50 μM), Shigella dysentariae ATCC 9752 (MIC > 100 μM), Salmonella typhimurium ATCC 14028 (MIC > 100 μM), Klebsiella pneumonia ATCC 10031 (MIC = 100 μM), Pseudomonas aeruginosa ATCC 27853 (MIC > 100 μM).

    • Hemolytic Activity

      • It has 0.65%, 0.60%, 0.59%, 0.76%, 0.83%, 0.76%, 0.88% and 1.04% hemolysis against human red blood cells at 0.8, 1.6, 3.1, 6.3, 12.5, 25.0, 50.0 and 100.0 μM.

    • 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: 2 and 6) in sequence indicates (S)-α-methyl, α-pentenylglycine. Note: the Experimental section presenst that X is (S)-α-methyl, α-pentenylglycine, while the Results section presents that X is pentenylalanine. We incline to the former representation according to previous papers published by the research group which the author belonged. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.

    • Stereochemistry

    • L

    • Secondary Structure

    • α-helix in 25 mM potassium phosphate buffer solution (pH 6.5)

    • Structure Description

    • As expected, in the far ultraviolet circular dichroism (CD) experiment, the stapled heptapeptides displayed enhanced helical contents compared to their corresponding unstapled counterparts.

    • Helical Wheel Diagram

    • DRAMP21613 helical wheel diagram

    • Predicted Structure

Literature Information

  • Literature 1

    • Title

    • De Novo Design and Their Antimicrobial Activity of Stapled Amphipathic Helices of Heptapeptides

    • Reference

    • B KOREAN CHEM SOC

    • Author

    • Thuy T.T. Dinh, Do-Hee Kim, Song-Jin Lee, Young-Woo Kim