General Information

    • DRAMP ID

    • DRAMP21624

    • Peptide Name

    • V30-SP-8

    • Sequence

    • ⓍLAAⒿRHⓍ

    • Sequence Length

    • 8

    • Original Sequence

    • ELAAIRHR

    • Source

    • Synthetic construct

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+

    • Comments

    • Function: Antibacterial activity against Gram-positive bacteria. The peptide shows a similar potency to vancomycin (MIC50 = 20 μM against M.smegmatis)

    • Target Organism

      • [Ref.32840352] Gram-positive bacteria: Mycobacterium smegmatis (The antibacterial effects of V30-SP-8 are 36.9%, 42.7%, 50.9% and 55.4% at 6.25, 12.5, 25 and 50 μM, and MIC50 is between 12.5 μM and 25.0 μM)

    • Hemolytic Activity

      • [Ref.32840352] No hemolytic activity information found.

    • Cytotoxicity

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

Structure Information

    • Linear/Cyclic

    • Cyclic (Stapled)

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Free

    • Special Amino Acid and Stapling Position

    • ①The Ⓧ (position: 1 and 8) in sequence indicates S5 stapling amino acid. Note: S5 is (S)-pentenyl alanine. ②The Ⓙ (position: 5) in sequence is B5 stapling amino acid. Note: B5 is α-dipentenyl alanine. ③Ⓧ (1) and Ⓙ (5), Ⓙ (5) and Ⓧ (8) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple respectively.

    • Stereochemistry

    • L

    • Secondary Structure

    • 26.1% α-helix content in 50 μM aqueous solution [a mixture of water and acetonitrile (9:1, v/v)].

    • Structure Description

    • ①The helical propensities of two stapled peptides, V30-SP-8 and V30-SP-9, and their linear counterparts were analyzed via circular dichroism (CD) spectrometry. ②Surprisingly, in contrast to our expectation that the stitched peptide, V30-SP-8, would be more helical than the monostapled peptide, V30-SP-9, the monostapling strategy was more effective in inducing helicity (helicity: 26.1% for V30-SP-8 and 33.8% for V30-SP-9)

    • Helical Wheel Diagram

    • DRAMP21624 helical wheel diagram

    • Predicted Structure

Literature Information

  • Literature 1

    • Title

    • Structure-Based De Novo Design of Mycobacterium Tuberculosis VapC-Activating Stapled Peptides

    • Reference

    • ACS Chem Biol. 2020 Sep 18;15(9):2493-2498. doi: 10.1021/acschembio.0c00492. Epub 2020 Sep 9.

    • Author

    • Sung-Min Kang, Heejo Moon, Sang-Woo Han, Do-Hee Kim, Byeong Moon Kim, Bong-Jin Lee