General Information

    • DRAMP ID

    • DRAMP21558

    • Peptide Name

    • KKK

    • Sequence

    • KⓍWKJⓍK

    • Sequence Length

    • 7

    • Original Sequence

    • /

    • 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

      • [Ref.30361948] Gram-positive bacteria: Bacillus subtilis ATCC 6633 (MIC = 12.5 μM), Staphyolococcus aureus ATCC 6538p (MIC = 6.3 μM), Staphylococcus epidermidis ATCC 12228 (MIC= 25 μM);
      • Gram-negative bacteria: Escherichia coli ATCC 25922 (MIC = 12.5 μM), Shigella dysenteriae ATCC 9752 (MIC = 25 μM), Salmonella typhimurium ATCC 14028 (MIC = 50 μM), Klebsiella pneumoniae ATCC 10031 (MIC = 18.8 μM), Pseudomonas aeruginosa ATCC 27853 (MIC = 25 μM).
      • [Ref.28547390] Gram-positive bacteria: Bacillus subtilis (MIC = 6.3 μg/mL), Staphylococcus aureus (MIC = 6.3 μg/mL), Staphylococcus epidermidis (MIC = 12.5 μg/mL);
      • Gram-negative bacteria: Escherichia coli (MIC = 12.5 μg/mL), Shigella dysenteriae (MIC = 12.5 μg/mL), Salmonella typhimurium (MIC = 50 μg/mL), Klebsiella pneumoniae (MIC = 18.8 μg/mL), Pseudomonas aeruginosa (MIC = 12.5 μg/mL).

    • Hemolytic Activity

      • [Ref.30361948] It has 1.5% hemolysis against human red blood cells at 25 μM and 3.0% hemolysis at 50 μM.
      • [Ref.28547390] 3.3% hemolysis against human red blood cells at 25 μM and 7.9% hemolysis t 50 μM.

    • 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: 5) in sequence is norleucine. ②The Ⓧ (position: 2 and 6) indicates (S)-α-methyl, α-pentenylglycine. ③Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.

    • Stereochemistry

    • L

    • Secondary Structure

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

    • Structure Description

    • ①[Ref.30361948] All analogs displayed similar CD spectra to that of KKK, having two minima near 208 and 222 nm and a maximum near 190nm, which are characteristic of α-helices. ②[Ref.28547390] Peptide NLE and LYS maintained a compatible helicity to LEU.

    • Helical Wheel Diagram

    • DRAMP21558 helical wheel diagram

    • Predicted Structure

    • There is no predicted structure for DRAMP21558.

Physicochemical Information

    • Formula

    • C₄₉H₈₁N₁₁O₈

    • Absent Amino Acids

    • ACDEFGHILMNPQRSTV

    • Common Amino Acids

    • K

    • Mass

    • 952.26

    • PI

    • /

    • Basic Residues

    • 3

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 1

    • Hydrophobicity

    • /

    • Polar Residues

    • 0

DRAMP21558

Literature Information

  • Literature 1

    • Title

    • Effects of lysine-to-arginine substitution on antimicrobial activity of cationic stapled heptapeptides.

    • Reference

    • Arch Pharm Res. 2018 Nov;41(11):1092-1097. doi: 10.1007/s12272-018-1084-5. Epub 2018 Oct 25.

    • Author

    • Huy X Luong, Do-Hee Kim, Bong-Jin Lee, Young-Woo Kim.
  • Literature 2

    • Title

    • Mono-substitution effects on antimicrobial activity of stapled heptapeptides.

    • Reference

    • Arch Pharm Res. 2017 Jun;40(6):713-719. doi: 10.1007/s12272-017-0922-1. Epub 2017 May 25.

    • Author

    • Huy X Luong, Do-Hee Kim, Ngoan T Mai, Bong-Jin Lee, Young-Woo Kim