General Information
DRAVP ID DRAVPe01792
Peptide Name VG-Chol
Sequence VALDPIDISIVLNKAKSDLEESKEWIRRSNGKLDSIGSGSGX
Sequence Length 42
UniProt ID No entry found
Source Synthetic construct
Activity Information
Target Organism HPIV 3
Assay Plaque reduction assay
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity
Binding Target membrane
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.
Structure Information
PDB ID None
Predicted Structure Download No predicted structure available
Linear/Cyclic Linear
N-terminal Modification Acetylation
C-terminal Modification Amidation
Other Modification The 'X' at position 42 indicates cholesterol-conjugated cysteine.
Stereochemistry L
Physicochemical Information
Formula C190H316N54O64
Absent amino acids CFHMQTY
Common amino acids S
Mass 4510.27
Pl 5.05
Basic residues 6
Acidic residues 7
Hydrophobic residues 14
Net charge -1
Boman Index -8236
Hydrophobicity -38.33
Aliphatic Index 102.14
Half Life
Extinction Coefficient cystines 5500
Absorbance 280nm 134.15
Polar residues 13
Literature Information
Literature 1
Title Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides
Pubmed ID 28344321
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