General Information


DRAVP ID  DRAVPe01282

Peptide Name   a-p9

Sequence  LMRIRQMMT

Sequence Length  9

UniProt ID  No entry found

Source  Synthetic construct



Activity Information


Target Organism  PRRSV

Assay  MTT assay

Activity 

  • [Ref.22743126]Porcine reproductive and respiratory syndrome virus(PRRSV):inhibition of PRRSV replication in MARC-145 cells(IC50=263.8101 μM).

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

Cytotoxicity 

  • [Ref.22743126]MARC-145 cells:CC50>500 μM.

Binding Target  PRRSV polymerase

Mechanism  PRRSV polymerase is an RNA-dependent RNA polymerase and is an enzyme specific to viruses, RNA-dependent RNA polymerase is one of the most important proteins for intracellular replication of viruses.The peptide could exert antiviral activity by inhibiting polymerase.



Structure Information


PDB ID  None

Predicted Structure Download  DRAVPe01282

Linear/Cyclic  Linear

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  None

Stereochemistry  L



Physicochemical Information


Formula  C48H90N16O12S3

Absent amino acids  ACDEFGHKNPSVWY

Common amino acids  M

Mass  1179.52

Pl  12

Basic residues  2

Acidic residues  0

Hydrophobic residues  2

Net charge  2

Boman Index  -2106

Hydrophobicity  8.89

Aliphatic Index  86.67

Half Life 

  •     Mammalian:5.5 hour
  •     Yeast:3 min
  •     E.coli:2 min

Extinction Coefficient cystines  0

Absorbance 280nm  0

Polar residues  1



Literature Information


Literature 1

Title   Antiviral activity of phage display selected peptides against Porcine reproductive and respiratory syndrome virus in vitro.

Pubmed ID   22743126

Reference   Virology. 2012 Oct 10;432(1):73-80.

Author   Liu K, Feng X, Ma Z, Luo C, Zhou B, Cao R, Huang L, Miao D, Pang R, He D, Lian X, Chen P. 

DOI   10.1016/j.virol.2012.05.010