General Information
DRAVP ID DRAVPe02323
Peptide Name CP3
Sequence SGWIYWAV
Sequence Length 8
UniProt ID No entry found
Taxon ID None
Source Designed In-silico on VEGAZZ software
Validation In-Silico
Origin Information
Gene Name/ID Not Available
GenBank Not Available
Amino Acid position Not Available
Domain Accession ID Not Available
Nucleotide sequence ID Not Available
Molecular Type Not Available
Chromosomal Position Not Available
Activity Information
Target Organism EBOV
Assay N/A
Activity
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 VP40.
Mechanism CP3, a cyclic peptide inhibitor, can inhibit Ebola virus budding by preventing the binding of UEV domain proteins to the P6 motif. CP3 forms hydrogen bonds with UEV domain proteins through its Tyr147 and Trp148 residues. Additionally, its Trp145, Tyr147, Ile146, and Trp148 residues engage in nonbonding interactions with UEV domain proteins. These interactions suggest that CP3 effectively disrupts the protein-protein interactions essential for the budding of both Ebola viruses.
Structure Information
PDB ID None
Linear/Cyclic Cyclic
N-terminal Modification Free
C-terminal Modification Free
Other Modification None
Stereochemistry L
Physicochemical Information
Formula C50H64N10O11
Absent amino acids CDEFHKLMNOPQRTU
Common amino acids W
Mass 981.12
Pl 5.24
Basic residues 0
Acidic residues 0
Hydrophobic residues 5
Net charge 0
Boman Index -1.6
Hydrophobicity 0.775
Aliphatic Index 97.5
Half Life
Extinction Coefficient cystines 12490
Absorbance 280nm 12.37
Polar residues 2
Literature Information
Literature 1
Title Cyclic Peptide Inhibitors of the Tsg101 UEV Protein Interactions Refined through Global Docking and Gaussian Accelerated Molecular Dynamics Simulations
Pubmed ID 32998394
Reference Polymers (Basel). 2020;12(10)
Author Lin WW, Wang YJ, Ko CW, et al