DRAVP ID  DRAVPe02034

Peptide Name   NOVEL-1

Sequence  NASDMEIKKVNKKIEEYIKKIEEVEKKLEEVNKK

Sequence Length  34

UniProt ID  No entry found

Taxon ID  None

Source  Synthetic Construct

Validation   Experimentally Validated

Gene Name/ID  HR1, HR2

GenBank  AAS00690, AAK27168

Amino Acid position  Not available

Domain Accession ID  Not Available

Nucleotide sequence ID  Not Available

Molecular Type  Not Available

Chromosomal Position  Not Available

Target Organism  NDV, IBV

Assay  Fusion Assay

Activity 

• [Ref. 21601229]NDV:Inhibition by NOVEL-1 and NOVEL-2 (~90% inhibition at 5 μM, plaque formation inhibition at 25 μM).
• IBV:Inhibition by NOVEL-1 and NOVEL-2 (~90% inhibition at 5 μM, plaque formation inhibition at 25μM).

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  Spike Protein

Mechanism  Entry inhibition, The novel peptides completely inhibited single virus infections and mixed infections caused by NDV and IBV. Furthermore, we assessed cell toxicity and possible targets for the peptides, thereby strengthening the notion that HR2 is an attractive site for therapeutic intervention. These results suggest the possibility of designing a relatively broad-spectrum class of antiviral peptides that can reduce the effects of mixed-infections. The novel peptides completely inhibited single virus infections and mixed infections caused by NDV and IBV. Furthermore, we assessed cell toxicity and possible targets for the peptides, thereby strengthening the notion that HR2 is an attractive site for therapeutic intervention. These results suggest the possibility of designing a relatively broad-spectrum class of antiviral peptides that can reduce the effects of mixed-infections.The novel peptides completely inhibited single virus infections and mixed infections caused by NDV and IBV. Furthermore, we assessed cell toxicity and possible targets for the peptides, thereby strengthening the notion that HR2 is an attractive site for therapeutic intervention. These results suggest the possibility of designing a relatively broad-spectrum class of antiviral peptides that can reduce the effects of mixed-infections.The novel peptides completely inhibited single virus infections and mixed infections caused by NDV and IBV. Furthermore, we assessed cell toxicity and possible targets for the peptides, thereby strengthening the notion that HR2 is an attractive site for therapeutic intervention. These results suggest the possibility of designing a relatively broad-spectrum class of antiviral peptides that can reduce the effects of mixed-infections.The novel peptides completely inhibited single virus infections and mixed infections caused by NDV and IBV. Furthermore, we assessed cell toxicity and possible targets for the peptides, thereby strengthening the notion that HR2 is an attractive site for therapeutic intervention. These results suggest the possibility of designing a relatively broad-spectrum class of antiviral peptides that can reduce the effects of mixed-infections.The novel peptides completely inhibited single virus infections and mixed infections caused by NDV and IBV. Furthermore, we assessed cell toxicity and possible targets for the peptides, thereby strengthening the notion that HR2 is an attractive site for therapeutic intervention. These results suggest the possibility of designing a relatively broad-spectrum class of antiviral peptides that can reduce the effects of mixed-infections.

PDB ID  None

Predicted Structure Download  No predicted structure available

Linear/Cyclic  Cyclic

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  None

Stereochemistry  L

Literature 1

Title   Characterisation and evaluation of antiviral recombinant peptides based on the heptad repeat regions of NDV and IBV fusion glycoproteins

Pubmed ID   21601229

Reference   Virology, 416(1-2), 65–74.

Author   Wang, X. J., Li, C. G., Chi, X. J., & Wang, M. (2011).

DOI   10.1016/j.virol.2011.05.001