Peptide name : Mastoparan-Cimals. XXA; UCLL1c)

Source/Organism : Venom, the European Hornet

Linear/Cyclic : Cyclic

Chirality : Not found

Peptide length: 14

C-terminal modification: Cyclic

N-terminal modification : Amidation

Non-natural peptide information: None

Assay type : MTT cell viability assay and Lactate dehydrogenase (LDH) leakage assay

Assay time : 24h

Activity : IC50 : < 4 μM

Cell line : U251-MG

Cancer type : Glioma

Other activity : Not found

Amino acid composition bar chart :

Molecular mass : 1507.9451 Dalton

Aliphatic index : 2.092

Instability index : 10.9143

Hydrophobicity (GRAVY) : 1.2786

Isoelectric point : 10.302

Charge (pH 7) : 2.7571

Aromaticity : 0

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

Hydrophobic/hydrophilic ratio : 2.5

hydrophobic moment : -0.959

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

Most occurring amino acid : L

Most occurring amino acid frequency : 5

Least occurring amino acid : N

Least occurring amino acid frequency : 1

Secondary structure fraction (Helix, Turn, Sheet): (0.7, 0.0, 0.5)

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

1 : Chen X, et al. Evaluation of the bioactivity of a mastoparan peptide from wasp venom and of its analogues designed through targeted engineering. Int J Biol Sci. 2018; 14:599-607. doi: 10.7150/ijbs.23419

Paper title : Evaluation of the bioactivity of a mastoparan peptide from wasp venom and of its analogues designed through targeted engineering.

Doi : https://doi.org/10.7150/ijbs.23419

Abstract : Mastoparan is a typical cationic and amphipathic tetradecapeptide found in wasp venom and exhibits potent biological activities. Yet, compared with other insect-derived peptides, such as melittin from the bee venom, this family have been underrated. Herein, we evaluated the biological activities of mastoparan-C (MP-C), which was identified from the venom of the European Hornet (Vespa crabro), and rationally designed two analogues (a skeleton-based cyclization by two cysteine residues and an N-terminal extension via tat-linked) for enhancing the stability of the biological activity and membrane permeability, respectively. Three peptides possessed broadly efficacious inhibiting capacities towards common pathogens, resistant strains, as well as microbial biofilm. Although, cyclized MP-C showed longer half-life time than the parent peptide, the lower potency of antimicrobial activity and higher degree of haemolysis were observed. The tat-linked MP-C exhibited more potent anticancer activity than the parent peptide, but it also loses the specificity. The study revealed that MP-C is good candidate for developing antimicrobial agents and the targeted-design could improve the stability and transmembrane delivery, but more investigation would be needed to adjust the side effects brought from the design.