General Information

    • DRAMP ID

    • DRAMP21578

    • Peptide Name

    • Val-HSLP

    • Sequence

    • WWVⓍARAⓍRR

    • Sequence Length

    • 10

    • Original Sequence

    • WWVXARAXRR

    • Source

    • Synthetic construct

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 20 μM.

    • Target Organism

      • [Ref.28073163] Gram-positive bacteria: Bacillus megaterium ATCC 14581 (IC50 = 0.69 μM, MIC = 5.00 μM), Staphylococcus aureus ATCC 6538 (IC50 = 0.63 μM, MIC = 5.00 μM), Enterococcus faecalis ATCC 29212 (IC50 = 0.65 μM, MIC = 5.00 μM);
      • Gram-negative bacteria: Escherichia coli ATCC 700926 (IC50 = 14.8 μM, MIC > 20 μM);
      • Fungi: Candida albicans 002 ATCC 64385 (IC50 > 20 μM, MIC > 20 μM), C. albicans 004 ATCC MYA-2876 (IC50 > 20 μM, MIC > 20 μM).

    • Hemolytic Activity

      • [Ref.28073163] HC50 = 14.5 μM against human red blood cells. Note: HC50 is the half-maximal hemolytic concentration.

    • Cytotoxicity

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

Structure Information

    • Linear/Cyclic

    • Cyclic (Stapled)

    • N-terminal Modification

    • Acylation (Valerylamide)

    • C-terminal Modification

    • Amidation

    • Special Amino Acid and Stapling Position

    • ①The Ⓧ (position: 4 and 8) in sequence indicates (S)-2-(4'-pentenyl)-alanine. ②Ⓧ (4) and Ⓧ (8) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.

    • Stereochemistry

    • L

    • Secondary Structure

    • 0.0% α-helix and 34.3% β-strand in 20 mM potassium phosphate buffer; 0.8% α-helix and 36.9% β-strand in 20 mM potassium phosphate buffer made 30% in TFE.

    • Structure Description

    • Only slghtly higher β-strand characteristics were observed for the hydrocarbon-stapled peptides in 30% TFE. Overall, the peptides showed some β-strand secondary structural characteristics and little α-helical content.

    • Helical Wheel Diagram

    • DRAMP21578 helical wheel diagram

    • Predicted Structure

Literature Information

  • Literature 1

    • Title

    • Hydrocarbon-stapled lipopeptides exhibit selective antimicrobial activity

    • Reference

    • Biopolymers. 2017 May;108(3). doi: 10.1002/bip.23006.

    • Author

    • Zachary B Jenner, Christopher M Crittenden, Martín Gonzalez, Jennifer S Brodbelt, Kerry A Bruns