General Information
DRAVP ID DRAVPe02232
Peptide Name C3LB-HA
Sequence GYHHQNEQGSGYAADLK
Sequence Length 17
UniProt ID No entry found
Taxon ID None
Source Synthetic construct
Validation Experimentally Validated
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 Influenza A H1N1/A/Puerto Rico/916/34 (H1N1)
Assay Cytopathic Effect inhibition
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity
Binding Target Hemagglutinin protein
Mechanism The binding to the HA, which prevents the conformational rearrangements inside the endosome, is the most likely mechanism of action.By in silico analysis of different HA1 and HA2, they discovered conserved regions (40–50 amino acids at the N- and C-terminal of HA1, and 80 amino acids at the N-terminal of HA2) that revealed short regions of HA1 N- and C-terminal ends characterized by hydrophilic, flexible, charged, and exposed (antigenic) sequences. Inhibitory activity of those peptides against IAV of various origins (human, swine, and avian) demonstrates the ability to inhibit IAV without cytotoxicity. The binding to the HA, which prevents the conformational rearrangements inside the endosome, is the most likely mechanism of action. Docking studies revealed that AVPs form several hydrogen bonds and electrostatic contacts in the HA stalk region with the fusion peptide, helix A, helix B, and loop B that could be responsible for the inhibition of HA conformational changes. Nevertheless, they did not show the stability at endosomal pH
Structure Information
PDB ID None
Linear/Cyclic Linear
N-terminal Modification Not included yet
C-terminal Modification Not included yet
Other Modification None
Stereochemistry L
Physicochemical Information
Formula C80H115N25O28
Absent amino acids RCIMFPTWVOU
Common amino acids G
Mass 1874.94
Pl 5.99
Basic residues 1
Acidic residues 2
Hydrophobic residues 3
Net charge -1
Boman Index 2.37
Hydrophobicity -1.471
Aliphatic Index 34.71
Half Life
Extinction Coefficient cystines 5500
Absorbance 280nm 1.589
Polar residues 5
Literature Information
Literature 1
Title Inhibition of influenza A virus infection in vitro by peptides designed in silico
Pubmed ID 24146939
Reference PloS one, 8(10), e76876.
Author López-Martínez, R., Ramírez-Salinas, G. L., Correa-Basurto, J., & Barrón, B. L. (2013).