• DRAMP ID

    • DRAMP29962
    • Peptide Name

    • Chol-VG
    • Source

    • Synthetic construct
    • Family

    • Paramyxoviridae
    • Gene

    • Not found
    • Sequence

    • XGSGSGVALDPIDIAnti-SIVLNKAKSDLEESKEWIRRSNGKLDSI
    • Sequence Length

    • 42
    • UniProt Entry

    • No entry found
    • Protein Existence

    • Not found
    • Biological Activity

    • Antimicrobial, Antiviral
    • Target Organism

      • [Ref.28344321]Human parainfluenza viruse 3(HPIV 3): inhibition of virus infection in Vero cells(IC90=1.7 ± 0.42 nM,IC50=0.06 ± 0.035 nM).
    • Hemolytic Activity

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

      • [Ref.28344321]Vero cells: CC50=9000 nM.
    • Binding Target

    • membrane
    • Linear/Cyclic

    • Linear
    • N-terminal Modification

    • Acetylation
    • C-terminal Modification

    • Amidation
    • Nonterminal Modifications and Unusual Amino Acids

    • The 'X' at position 1 indicates cholesterol-conjugated cysteine.
    • Stereochemistry

    • L
    • Structure

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP29962 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP29962.
    • Formula

    • C190H316N54O64
    • Absent Amino Acids

    • CFHMQTY
    • Common Amino Acids

    • S
    • Mass

    • 4510.27
    • PI

    • 5.05
    • Basic Residues

    • 6
    • Acidic Residues

    • 7
    • Hydrophobic Residues

    • 14
    • Net Charge

    • -1
    • Boman Index

    • -8236
    • Hydrophobicity

    • -0.383
    • Aliphatic Index

    • 102.14
    • Half Life

      • Mammalian:
      • Yeast:
      • E.coli:
    • Extinction Coefficient Cystines

    • 5500
    • Absorbance 280nm

    • 134.15
    • Polar Residues

    • 13

DRAMP29962

DRAMP29962 chydropathy plot
    • Mechanism

    • Peptides derived from the HRC of paramyxovirus F proteins interfere with formation of the six-helix bundle in a dominant-negative manner by binding to the transiently exposed HRN coiled coil in the transient fusion intermediate, thereby inhibiting membrane fusion.
  • ·Literature 1
    • Title

    • Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides
    • Reference

    • Sci Rep. 2017 Mar 8;7:43610.
    • Author

    • Mathieu C, Augusto MT, Niewiesk S, Horvat B, Palermo LM, Sanna G, Madeddu S, Huey D, Castanho MA, Porotto M, Santos NC, Moscona A