• DRAMP ID

    • DRAMP30387
    • Peptide Name

    • M0
    • Source

    • Synthetic construct
    • Family

    • Coronaviridae
    • Gene

    • Not found
    • Sequence

    • TTLLDLTYEMLSLQQVVKALNESYIDLKEL
    • Sequence Length

    • 30
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Not found
    • Biological Activity

    • Antimicrobial, Antiviral
    • Target Organism

      • [Ref.27795416]MERS-CoV:inhibition of MERS-CoV S-medicated cell-cell fusion in MT-2 cells(IC50=4.5 μM);inhibition of pseudovirus infection in MT-2 cells(IC50=17.8 μM).
    • 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

    • DRAMP30387 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP30387.
    • Formula

    • C157H259N35O51S
    • Absent Amino Acids

    • CFGHPRW
    • Common Amino Acids

    • L
    • Mass

    • 3485.05
    • PI

    • 4.18
    • Basic Residues

    • 2
    • Acidic Residues

    • 5
    • Hydrophobic Residues

    • 12
    • Net Charge

    • -3
    • Boman Index

    • -2496
    • Hydrophobicity

    • 0.163
    • Aliphatic Index

    • 139.67
    • Half Life

      • Mammalian:7.2 hour
      • Yeast:>20 hour
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 2980
    • Absorbance 280nm

    • 102.76
    • Polar Residues

    • 8

DRAMP30387

DRAMP30387 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.