To the extent possible under law, the person who associated CC0 with this work has waived all copyright and related or neighboring rights to this work.
General Information
DRAVP ID DRAVPe02085
Peptide Name Defensins
Sequence ACYCRIPACIAGERRYGTCIYQGRLWAFCC
Sequence Length 30
UniProt ID None
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 IAV(H1N1,H3N2)
Assay Antiviral assay.
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 Membrane
Mechanism Inhibit Virus Attachment and Virus-Cell Membrane Fusion
Structure Information
PDB ID None
Predicted Structure Download No predicted structure available
Linear/Cyclic Linear
N-terminal Modification Free
C-terminal Modification Free
Other Modification None
Stereochemistry L
Physicochemical Information
Formula C150H228N44O38S6
Absent amino acids NDHKMSVOU
Common amino acids ARCGIY
Mass 3448.09
Pl 8.68
Basic residues 4
Acidic residues 1
Hydrophobic residues 13
Net charge 3
Boman Index 1.1704
Hydrophobicity 0.3
Aliphatic Index 65.33
Half Life
Extinction Coefficient cystines 10345
Absorbance 280nm 3
Polar residues 20
Literature Information
Literature 1
Title Interactions of alpha-, beta-, and theta-defensins with influenza A virus and surfactant protein D
Pubmed ID 19494312
Reference Journal of immunology (Baltimore, Md. : 1950), 182(12), 7878–7887.
Author Doss, M., White, M. R., Tecle, T., Gantz, D., Crouch, E. C., Jung, G., Ruchala, P., Waring, A. J., Lehrer, R. I., & Hartshorn, K. L. (2009).
To the extent possible under law, the person who associated CC0 with this work has waived all copyright and related or neighboring rights to this work.