• DRAMP ID

    • DRAMP30384
    • Peptide Name

    • WQ-IDL(628-656)
    • Source

    • Synthetic construct
    • Family

    • Retroviridae
    • Gene

    • Not found
    • Sequence

    • WEEWDKKIEEYTKKIEELIKKSQNQQIDL
    • Sequence Length

    • 29
    • Protein Existence

    • Not found
    • Biological Activity

    • Antimicrobial, Antiviral
    • Target Organism

      • [Ref.27795416]HIV-1 IIIB:inhibition of virus infection in MT-2 cells(IC50=1.6 ±0.1 nM); inhibition of peptide against cell-cell fusion between H9/HIV-1 IIIB cells and MT-2 cells(IC50=5.6± 1.2 nM);
      • HIV-1 Bal:inhibition of virus infection in MT-2 cells(IC50=2.5 ± 0.1 nM);
      • HIV-1 clinical isolates(8 clinical isolates):inhibition of virus infection in MT-2 cells(IC50=2.0-90.7 nM);
      • HIV-1 pseudoviruses(7 pseudoviruses):inhibition of pseudoviruses infection in MT-2 cells(IC50=0.8-37.4 nM);
      • HIV-1 T20-resistant strains(5 strains):inhibition of virus infection in MT-2 cells(IC50=1.6-22.0 nM);
      • HIV-1 T2635-resistant strain(6 strains):inhibition of virus infection in MT-2 cells(IC50=8.5-61.4 nM).
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

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

    • membrane
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Free
    • C-terminal Modification

    • Free
    • Nonterminal Modifications and Unusual Amino Acids

    • None
    • Stereochemistry

    • L
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP30384 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP30384.
    • Formula

    • C167H263N41O53
    • Absent Amino Acids

    • ACFGHMPRV
    • Common Amino Acids

    • EK
    • Mass

    • 3693.17
    • PI

    • 4.86
    • Basic Residues

    • 6
    • Acidic Residues

    • 8
    • Hydrophobic Residues

    • 8
    • Net Charge

    • -2
    • Boman Index

    • -8679
    • Hydrophobicity

    • -1.531
    • Aliphatic Index

    • 80.69
    • Half Life

      • Mammalian:2.8 hour
      • Yeast:3 min
      • E.coli:2 min
    • Extinction Coefficient Cystines

    • 12490
    • Absorbance 280nm

    • 446.07
    • Polar Residues

    • 4

DRAMP30384

DRAMP30384 chydropathy plot
    • Mechanism

    • The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation.
  • ·Literature 1
    • Title

    • Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.
    • Reference

    • J Virol. 2016 Dec 16;91(1):e01445-16.
    • Author

    • Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.