General Information

General Information

DRAVP ID DRAVPe00721

Peptide Name CPEM

Sequence CPEVFLM

Sequence Length 7

UniProt ID No entry found

Source Synthetic construct(derived from the C-terminal sequence of α1-antitrypsin)

Activity Information

Target Organism HIV

Assay

Activity

[Ref.22406118]HIV-1 IIIB:inhibition of virus replication(IC50>100 μM);inhibition of cell-cell fusion between H9/HIV-1IIIB cells and MT-2 cells(IC50>200 μM).

Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry

Cytotoxicity

[Ref.22406118]MT-2 cells:CC50>200 μM.

Binding Target Not found

Mechanism The cyclic peptide inhibited HIV-1 infection by blocking virus fusion with and entry into the target cells.

Structure Information

PDB ID None

Predicted Structure Download DRAVPe00721

Linear/Cyclic Cyclic

N-terminal Modification Cyclization (N termini to C termini)

C-terminal Modification Cyclization (N termini to C termini)

Other Modification None

Stereochemistry L

Physicochemical Information

Formula C38H59N7O10S2

Absent amino acids ADGHIKNQRSTWY

Common amino acids CEFLMPV

Mass 838.05

Pl 4

Basic residues 0

Acidic residues 1

Hydrophobic residues 3

Net charge -1

Boman Index 876

Hydrophobicity 144.29

Aliphatic Index 97.14

Half Life

Mammalian:1.2 hour
Yeast:>20 hour
E.coli:>10 hour

Extinction Coefficient cystines 0

Absorbance 280nm 0

Polar residues 1

Literature Information

Literature 1

Title Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity.

Pubmed ID 22406118

Reference Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5.

Author Jia Q, Jiang X, Yu F, Qiu J, Kang X, Cai L, Li L, Shi W, Liu S, Jiang S, Liu K.

DOI 10.1016/j.bmcl.2012.02.037