Peptide name : BmKn2

Source/Organism : Venom, Chinese scorpion

Linear/Cyclic : Linear

Chirality : L

Peptide length: 13

C-terminal modification: Linear

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Anti-microbial activity

Amino acid composition bar chart :

Molecular mass : 1448.7933 Dalton

Aliphatic index : 1.653

Instability index : -3.8308

Hydrophobicity (GRAVY) : 1.5923

Isoelectric point : 11.000

Charge (pH 7) : 1.7591

Aromaticity : 0.153

Molar extinction coefficient (cysteine, cystine): (0, 0)

Hydrophobic/hydrophilic ratio : 3.33333333

hydrophobic moment : 1.1381

Missing amino acid : C,W,H,Q,T,P,M,E,D,Y,N,V

Most occurring amino acid : I

Most occurring amino acid frequency : 3

Least occurring amino acid : G

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.3, 0.1, 0.5)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](C)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](N)Cc1ccccc1)[C@@H](C)CC)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](Cc1ccccc1)C(=O)O)[C@@H](C)CC

1 : Zeng XC, et al. Identification and functional characterization of novel scorpion venom peptides with no disulfide bridge from Buthus martensii Karsch. Peptides. 2004; 25:143-50. doi: 10.1016/j.peptides.2003.12.003

Paper title : Identification and functional characterization of novel scorpion venom peptides with no disulfide bridge from Buthus martensii Karsch.

Doi : https://doi.org/10.1016/j.peptides.2003.12.003

Abstract : The scorpion venom peptides with no disulfide bridge are rarely identified and poorly characterized so far. Here, we report the identification and characterization of four novel disulfide-bridge-free venom peptides (BmKa1, BmKa2, BmKb1 and BmKn2) from Buthus martensii Kasch. BmKa1 and BmKa2 are very acidic and hydrophilic, showing no any similarity to other proteins, whereas BmKb1 and BmKn2 both are basic, alpha-helical peptide with an amidated C-terminus, showing a little homology with other peptides. Functional tests with synthetic peptide showed that BmKn2 has strong antimicrobial activity against both Gram-positive and Gram-negative bacteria, whereas BmKb1 has weak activity in inhibiting the growth of these bacteria.