General Information

    • DRAMP ID

    • DRAMP28998

    • Peptide Name

    • Stapled heptapeptide 2

    • Sequence

    • RⓍWWRⓍW

    • Sequence Length

    • 7

    • Original Sequence

    • RWWWRWW

    • Source

    • Synthetic construct

    • SMILES

    • C[C@@]1(NC(=O)[C@@H]([NH3+])CCCNC(N)=[NH2+])CCCC=CCCC[C@@](C)(C(=O)N[C@@H](C=O)Cc2c[nH]c3ccccc23)NC(=O)[C@H](CCCNC(N)=[NH2+])NC(=O)[C@H](Cc2c[nH]c3ccccc23)NC(=O)[C@H](Cc2c[nH]c3ccccc23)NC1=O

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+

    • Comments

    • Function: Antibacterial activity against Gram-positive bacteria. The stapled peptide was much more active against bacteria than the unstapled one.

    • Target Organism

      • Gram-positive bacteria: Staphylococcus aureus ATCC25923 (MIC = 19 ± 4 μg/mL). Methicillin-resistant Staphylococcus aureus (MRSA) (MIC > 25 ± 6 μg/mL)

    • Hemolytic Activity

      • 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

    • Amidation

    • Special Amino Acid and Stapling Position

    • ①The Ⓧ (position: 2 and 6) in sequence indicate (S)-4-pentenyl alanine. ②Ⓧ (2) and Ⓧ (6) are cross-linked by hydrocarbon stapling through an oct-4-enyl hydrocarbon staple.

    • Stereochemistry

    • L

    • Secondary Structure

    • Helicity = 61.3% in 10 mM sodium phosphate buffer (pH 7.4) at peptide concentrations of 100 μM

    • Structure Description

    • CD spectroscopy was used to characterize the secondary structure of five unstapled heptapeptides and their stapled counterparts in phosphate buffer, indicating a significant increase in peptide helical content upon the stapling, with helicity change from h = 14.1% - 33.7% (for unstapled peptides) to h = 58.9%-75.1% (for stapled peptides).
  • There is no predicted structure for DRAMP28998.

Literature Information

  • Literature 1

    • Title

    • De Novo Hydrocarbon-Stapling Design of Single-Turn α-Helical Antimicrobial Peptides

    • Reference

    • Int J Pept Res Ther. 2019 Nov 14; 26(4):1711–1719. doi: 10.1007/s10989-019-09964-7.

    • Author

    • Zhixia Chen, Xiuli Yu, Aiying Zhang, Fangfang Wang, Yankun Xing