General Information


DRAVP ID  DRAVPe00454

Peptide Name   M2 NH

Sequence  RLAAKCAARFAEHGLKRG

Sequence Length  18

UniProt ID  No entry found

Source  Synthetic construct(derived from influenza virus M2 protein)



Activity Information


Target Organism  H1N1

Assay 

Activity 

  • [Ref.31375212]H1N1:did not exhibit any inhibitory effect.

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

Cytotoxicity 

  • [Ref.31375212]did not show apparent cytotoxicity against Madin-Darby canine kidney epithelial(MDCK) cells up to a concentration of 100 μM.

Binding Target  membrane

Mechanism  M2 NH is an α-helical amphipathic peptide with basic amino acids positioned at the polar-nonpolar interface. The peptide inserts deeply into the hydrophobic core of the membrane bilayer, resulting in alteration of membrane order and curvature . This ability to alter membrane curvature enables M2 NH to induce membrane budding in vitro and in vivo. It localizes to the neck of the budding virion and plays an important role in membrane scission.



Structure Information


PDB ID  None

Predicted Structure Download  DRAVPe00454

Linear/Cyclic  Linear

N-terminal Modification  Free

C-terminal Modification  Free

Other Modification  None

Stereochemistry  L



Physicochemical Information


Formula  C84H143N31O21S

Absent amino acids  DIMNPQSTVWY

Common amino acids  A

Mass  1955.31

Pl  10.92

Basic residues  6

Acidic residues  1

Hydrophobic residues  8

Net charge  5

Boman Index  -4230

Hydrophobicity  -38.33

Aliphatic Index  71.11

Half Life 

  •     Mammalian:1 hour
  •     Yeast:2 min
  •     E.coli:2 min

Extinction Coefficient cystines  0

Absorbance 280nm  0

Polar residues  3



Literature Information


Literature 1

Title   Envelope-deforming antiviral peptide derived from influenza virus M2 protein.

Pubmed ID   31375212

Reference   Biochem Biophys Res Commun. 2019 Sep 24;517(3):507-512.

Author   Jung Y, Kong B, Moon S, Yu SH, Chung J, Ban C, Chung WJ, Kim SG, Kweon DH. 

DOI   10.1016/j.bbrc.2019.07.088