General Information


DRAVP ID  DRAVPe02070

Peptide Name   BmKn2

Sequence  FIGAIARLLSKIF

Sequence Length  13

UniProt ID  None  

Taxon ID  34649 

Source  venom, Buthus martensii Karsch

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  HIV-1

Assay  Antiviral effect assay

Activity 

  • [Ref:22536342]HIV-1: BmKn2 and Kn2-7 decreased infectivity of HIV-1 clade B b12-resistant pseudotyped virus CAAN5342

Hemolytic Activity 

  • [Ref22536342] human RBC, HC50 12.5 ug/ml, hemolytic

Cytotoxicity  No cytotoxicity information found in the reference(s) presented

Binding Target  Not Found

Mechanism  BmKn2 aggregates and inserts into viral envelope so that the hydrophobic peptide region aligns with the lipid core region and the hydrophilic peptide regions form the interior region of the pore, with the help of positive charge of peptide somehow



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  While deletions of 1 to 4 residues from the peptide (Kn2-1 to Kn2-6) reduced its activity against S. aureus, peptide Kn2-7 (changes of G3, A4, and S10 to cationic K/R) showed increased activity due to an increase in cationicity. However, C-terminally truncated or cyclic BmKn2 lost activity against N. gonorrhoeae, indicating both the linear and intact sequence are important for peptide activity. 

Stereochemistry  L



Physicochemical Information


Formula  C71H117N17O15

Absent amino acids  NDCQEHMPTWYVOU

Common amino acids  I

Mass  1448.81

Pl  11

Basic residues  3

Acidic residues  0

Hydrophobic residues  10

Net charge  3

Boman Index  -0.86

Hydrophobicity  1.592

Aliphatic Index  165.38

Half Life 

  •     Mammalian:1.1 hours
  •     Yeast:3 mins
  •     E.coli:2 miins

Extinction Coefficient cystines  0

Absorbance 280nm  0

Polar residues  13



Literature Information


Literature 1

Title   Anti-HIV-1 activity of a new scorpion venom peptide derivative Kn2-7

Pubmed ID   22536342

Reference   PloS one, 7(4), e34947.

Author   Chen, Y., Cao, L., Zhong, M., Zhang, Y., Han, C., Li, Q., Yang, J., Zhou, D., Shi, W., He, B., Liu, F., Yu, J., Sun, Y., Cao, Y., Li, Y., Li, W., Guo, D., Cao, Z., & Yan, H. (2012).

DOI   10.1371/journal.pone.0034947