Mohammed H. M. Abdulrazzaq

(Assistant Lecturer)

Department of Conservation Agriculture

Center for Desert Studies

With over 5000 species, vespid wasps (Family: Vespidae) are found all over the world. Proteins, peptides (e.g., Mastoparan, Eumenitin, Eumenitin-R, Rumenitin-F, Epvp, Decoralin, and Anoplin (figure 1), enzymes (Hyaluronidase (Figure 2), α-Glucosidase, Phosphatase Phospholipase A2, And Phospholipase B), and small molecules are among the many different chemical components of wasp venom. Many advantageous properties, including antimicrobial, anticancer, and anti-inflammatory properties, have been demonstrated by the compounds that were extracted from wasp venom (Kim YangSeon et al., 2016). Nevertheless, trace amounts of their peptides have been reported. These molecules were developed and designed using solid phase peptide synthesis (SPPS). Several peptides, including Mastoparan, Anoplin, Decoralin, Polybia-MP-I, Polybia-CP, Polydim-I, and Agelaia-MP, were successfully synthesized using SPPS technology. Antimicrobial and anticancer properties are possessed by the synthetic peptides (Hilchie et al., 2016).

(Figure 1). Anoplin (C₅₄H₁₀₄N₁₆O₁₁)

(Figure 2) Hyaluronidase C₅₄H₁₀₄N₁₆O₁₁

Asthma, cancer, and arthritis are just a few of the debilitating conditions that have inflammation at their root. The current use of anti-inflammatory drugs suppresses both short-term and long-term bodily reactions, so finding new molecules with comparable characteristics is essential. Through the release of lipopolysaccharide (LPS), Vespa tropica venom stimulated microglia and successfully decreased oxidative stress. Treatment with wasp venom (5 and 10 µg/mL) significantly reduced the activation of NF-kB phosphorylation caused by LPS. Bracon hebetor venom (BHV) had an impact on septic shock in mouse models and LPS-induced nitric oxide (NO) in RAW 264.7 cells. Between 0.1 and 0.4 µg/mL, BHV significantly mediated LPS-induced inflammation without causing any cytotoxicity. At least 80 proteins are present in Nasonia vitripennis venom, which also has anti-inflammatory effects by inhibiting the production of the proinflammatory cytokine IL-1.

Mastoparan (MP) (figure 3), a primary constituent of P. jadwigae wasp venom, is a basic amphiphilic a-helical peptide with 14 amino acid residues, hydrophobic and essential amino acids, and an amino acid C-terminus. When in contact with bilayer phospholipids, these characteristics, which are unique to the cationic amphiphilic peptide (CAP) class, favor the α-helix conformation. MP exhibits a number of biological effects, including cytotoxicity on tumor cells, enhanced mast cell histamine release, and antimicrobial qualities. In a homogenous K562 cell, MP-induced mitochondrial permeability and a strong transition of mitochondrial permeability (PT) within a range of 25 µM were documented. Additionally, MP has anticancer effects on breast cancer, myeloma, and leukemia cells (Yamada et al., 2005). MP and the medication gemcitabine had a synergistic effect in a mouse model of mammary carcinoma. With doses ranging from 77.9 to 432.5 µM, MP demonstrated dose-dependent activity against human cancer cells, including MCF-7, MDAMB-231, Jurkat (T cell leukemia), SiHa (cervical carcinoma), A2058 (melanoma), and SK-BR-3 (breast cancer). B16F10 murine melanoma had an IC50 of 165 µM. In MP-induced apoptosis, caspases -9, -12, and -3 are activated, PARP is cleaved, pro-apoptotic Bax and Bim are upregulated, anti-apoptotic Bcl-XL is downregulated, and mitochondrial membrane disruption is brought on by cell apoptosis(de Azevedo et al., 2015).

(Figure 3). Mastoparan (C₇₀H₁₃₁N₁₉O₁₅)

Reference

de Azevedo, R. A., Figueiredo, C. R., Ferreira, A. K., Matsuo, A. L., Massaoka, M. H., Girola, N., Auada, A. V. V, Farias, C. F., Pasqualoto, K. F. M., & Rodrigues, C. P. (2015). Mastoparan induces apoptosis in B16F10-Nex2 melanoma cells via the intrinsic mitochondrial pathway and displays antitumor activity in vivo. Peptides, 68, 113–119.

Hilchie, A. L., Sharon, A. J., Haney, E. F., Hoskin, D. W., Bally, M. B., Franco, O. L., Corcoran, J. A., & Hancock, R. E. W. (2016). Mastoparan is a membranolytic anti-cancer peptide that works synergistically with gemcitabine in a mouse model of mammary carcinoma. Biochimica Et Biophysica Acta (BBA)-Biomembranes, 1858(12), 3195–3204.

Kim YangSeon, K. Y., Son MinKy, S. M., Noh EunYoung, N. E., Kim SooNok, K. S., Kim ChangMu, K. C., Yeo JooHong, Y. J., Park ChaNin, P. C., Lee KeunWoo, L. K., & Bang WooYoung, B. W. (2016). MP-V1 from the venom of social wasp Vespula vulgaris is a de novo type of mastoparan that displays superior antimicrobial activities.

Yamada, Y., Shinohara, Y., Kakudo, T., Chaki, S., Futaki, S., Kamiya, H., & Harashima, H. (2005). Mitochondrial delivery of mastoparan with transferrin liposomes equipped with a pH-sensitive fusogenic peptide for selective cancer therapy. International Journal of Pharmaceutics, 303(1–2), 1–7.

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