Peptide name : Mastoparan B

Source/Organism : Hornet

Linear/Cyclic : Linear

Chirality : L

Peptide length: 14

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 : Colorectal cancer

Other activity : Anti-bacterial activity

Amino acid composition bar chart :

Molecular mass : 1613.0393 Dalton

Aliphatic index : 1.6

Instability index : -31.771

Hydrophobicity (GRAVY) : 0.5714

Isoelectric point : 10.477

Charge (pH 7) : 3.7561

Aromaticity : 0.071

Molar extinction coefficient (cysteine, cystine): (5500, 5500)

Hydrophobic/hydrophilic ratio : 1.33333333

hydrophobic moment : -1.376

Missing amino acid : C,R,H,Q,T,P,M,E,F,D,Y,N,G

Most occurring amino acid : K

Most occurring amino acid frequency : 4

Least occurring amino acid : I

Least occurring amino acid frequency : 1

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

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)O)C(C)C)C(C)C

1 : Park NG, et al. Interaction of mastoparan-B from venom of a hornet in Taiwan with phospholipid bilayers and its antimicrobial activity. Biopolymers. 1995; 36:793-801. doi: 10.1002/bip.360360611

Paper title : Interaction of mastoparan-B from venom of a hornet in Taiwan with phospholipid bilayers and its antimicrobial activity.

Doi : https://doi.org/10.1002/bip.360360611

Abstract : Mastoparan B (MP-B), an amphiphilic alpha-helical peptide newly isolated from the hornet Vespa basalis, was studied in comparison with mastoparan (MP), in terms of interaction with the phospholipid bilayer and of hemolytic and antimicrobial activity. The amphiphilic structure of MP-B has more hydrophilic amino acid residues in the hydrophilic surface than that of MP. Although each peptide had a considerably different effect on the interaction with lipid bilayers (e.g., their conformation in the presence of acidic and of neutral lipids and dye-release ability from the encapsulated liposomes), on the whole the interaction mode was similar. MP-B caused a change in the shape of erythrocytes from normal discoid to a crenated form (named echinocytes). MP exhibited strong activity against gram-positive bacteria but not against gram-negative ones. Contrary to this, MP-B showed both strong activity against gram-positive bacteria and potent activity against gram-negative bacteria. Whereas both peptides have almost the same residues on the hydrophobic side, the difference in the hydrophilic surface area on the molecules seems to lead to the subtle change in its interaction with membranes, resulting in the alteration of biological activity.