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 DRAVPe00129
Peptide Name VMI16
Sequence SPYPSWSTPAGR
Sequence Length 12
UniProt ID No entry found
Source Synthetic construct(phage display)
Activity Information
Target Organism HIV
Assay Affinity binding assay
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity
Binding Target Vif proteins
Mechanism Vif proteins are essential for HIV-1 replication and able to form multimer, which is critical to the biological activity of many prokaryotic and eukaryotic proteins and is a common mechanism for the functional activation/inactivation of proteins.The peptide could bind with vif proteins and block the multimerization of them,which should inhibit HIV-1 replication.
Structure Information
PDB ID None
Predicted Structure Download DRAVPe00129
Linear/Cyclic Linear
N-terminal Modification Free
C-terminal Modification Free
Other Modification None
Stereochemistry L
Physicochemical Information
Formula C59H84N16O18
Absent amino acids CDEFHIKLMNQV
Common amino acids PS
Mass 1305.41
Pl 8.46
Basic residues 1
Acidic residues 0
Hydrophobic residues 2
Net charge 1
Boman Index -2275
Hydrophobicity -110
Aliphatic Index 8.33
Half Life
Extinction Coefficient cystines 6990
Absorbance 280nm 635.45
Polar residues 6
Literature Information
Literature 1
Title Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins.
Pubmed ID 12480936
Reference J Biol Chem. 2003 Feb 21;278(8):6596-602.
Author Yang B, Gao L, Li L, Lu Z, Fan X, Patel CA, Pomerantz RJ, DuBois GC, Zhang H.
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.