General Information

    • DRAMP ID

    • DRAMP21621

    • Peptide Name

    • sKFGF

    • Sequence

    • AAⓀLLPⒹLLAAP

    • Sequence Length

    • 12

    • Original Sequence

    • AAVLLPVLLAAP

    • 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.28921993] Gram-positive bacteria: Staphylococcus aureus (MIC > 256 μg/mL), Enterococcus faecalis (MIC > 256 μg/mL);
      • Gram-negative bacteria: Escherichia coli (MIC > 256 μg/mL), Pseudomonas aeruginosa (MIC > 256 μg/mL)

    • Hemolytic Activity

      • [Ref.28921993] It has 0.4%, 0%, 0.1%, 0.2%, 0.1%, 0.7%, 1.8% and 5.6% hemolysis against human red blood cells at 5, 7.5, 10, 15, 20, 25, 30 and 40 μg/ml.

    • Cytotoxicity

      • [Ref.28921993] The toxicity of sKFGF toward HEK293 and HeLa cells is much less than nonaarginine (R9) by use of flow cytometry and the peptide doesn't show any cytotoxicity at 2 μM.

Structure Information

    • Linear/Cyclic

    • Cyclic (Stapled)

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Amidation

    • Special Amino Acid and Stapling Position

    • Ⓚ (3) and Ⓓ (7) are cross-linked by lactam stapling through the polar amide bond of a lactam bridge.

    • Stereochemistry

    • L

    • Secondary Structure

    • ①Disordered (or unstructured) conformation in aqueous solutions [pure water (H₂O), phosphate buffer (PB, 10 mM), and phosphate buffer with high salt (NaF, 100 mM)]. ②Around 22% average α-helix content in various membranes environments [13% in POPC; 32% in

    • Structure Description

    • In the cases of sDRIM and sKFGF, stapling did not induce any conformational change, as these analogues remained just as unstructured.

    • Helical Wheel Diagram

    • DRAMP21621 helical wheel diagram

    • Predicted Structure

    • There is no predicted structure for DRAMP21621.

Physicochemical Information

    • Formula

    • C₅₆H₉₆N₁₂O₁₂

    • Absent Amino Acids

    • CEFGHIMNQRSTVWY

    • Common Amino Acids

    • AL

    • Mass

    • 1129.46

    • PI

    • /

    • Basic Residues

    • 1

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 8

    • Hydrophobicity

    • /

    • Polar Residues

    • 0

DRAMP21621

Literature Information

  • Literature 1

    • Title

    • Lactam-Stapled Cell-Penetrating Peptides: Cell Uptake and Membrane Binding Properties.

    • Reference

    • J Med Chem. 2017 Oct 12;60(19):8071-8082. doi: 10.1021/acs.jmedchem.7b00813. Epub 2017 Sep 26.

    • Author

    • Marco J Klein, Samuel Schmidt, Parvesh Wadhwani, Jochen Bürck, Johannes Reichert, Sergii Afonin, Marina Berditsch, Tim Schober, Roland Brock, Manfred Kansy, Anne S Ulrich