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Animal Source Foods
Published in Chuong Pham-Huy, Bruno Pham Huy, Food and Lifestyle in Health and Disease, 2022
Chuong Pham-Huy, Bruno Pham Huy
Honeybee venom and its major component melittin, an amphipathic 26-amino-acid-peptide, have demonstrated antitumoral effects in breast cancer, melanoma, non-small-cell lung cancer, glioblastoma, leukemia, ovarian, cervical, and pancreatic cancers, with higher cytotoxic potency in cancer cells compared to non-transformed cells (172).
Biology and Distribution of Hymenopterans of Medical Importance, Their Venom Apparatus and Venom Composition
Published in Jürg Meier, Julian White, Handbook of: Clinical Toxicology of Animal Venoms and Poisons, 2017
About fifty percent of the dry venom of bees is melittin, a peptide consisting of twenty-six amino acids, free of sulphur. The distribution of the amino acids in the molecule is quite remarkable, since non-polar, hydrophobic and neutral amino acids are found in the N-terminal part, whereas the polar, hydrophilic and basic amino acids are concentrated in its C-terminal part. Thus, the molecule exerts amphiphilic properties and is, like lysolecithin, a natural detergent with a high activity towards membranes. Melittin is responsible for the pain involved in bee stings. In cell membranes, melittin forms tetrameric pores that facilitate ion diffusion. The melittin-tetrameres lead to a breakdown of the resting potential, which initiates the sensation of pain.
Intestinal Chloride Secretion: Cyclic Amp and Ca2+ Interactions
Published in T. S. Gaginella, Regulatory Mechanisms — in — Gastrointestinal Function, 2017
Vincenzo Calderaro, Francesco Rossi
p-Bromophenacyl bromide is an alkylating agent largely used as PLA 2inhibitor in in vitro studies, but it lacks specificity since it may also irreversibly inhibit adenylyl cyclase activity.206 Specific inhibitors of PLA2 have been derived from phospholipid analogues, but they have manifested cytotoxic effects. Monoalide and monoalogue have been shown to inhibit melittin PLA2 by an irreversible mechanism as a result of covalent modification of lysine residues.207,208
Antinociceptive peptides from venomous arthropods
Published in Toxin Reviews, 2023
Jessica A. I. Muller, Lai Y. Chan, Monica C. Toffoli-Kadri, Marcia R. Mortari, David J. Craik, Johannes Koehbach
Melittin is the major component of the A. mellifera venom from bees and is responsible for most of the activities observed with the whole venom. This peptide, when injected s.c. shows antinociceptive activity in the paclitaxel‐induced mechanical hyperalgesia (Choi et al.2017) and reduced mechanical and cold allodynia (Choi et al.2019). The mechanism of action in these assays involves spinal α2-adrenergic receptor (Choi et al.2017). When injected s.c., melittin reduced the licking time in the second phase of the formalin (inflammatory pain) (Merlo et al.2011) and acetic acid assays (Kwon et al.2005); however, if the animal is not stimulated with a pain inducer, melittin can itself induce pain when injected via i.pl. (Merlo et al.2011). Therefore, more assays are necessary to better characterize these effects. Current literature shows that this peptide can present an antinociceptive potential when the murine model has a previous pain and/or inflammatory process, but it can also induce pain if the animal does not present a condition of nociception (Chen and Lariviere 2010).
Cellular targets and molecular activity mechanisms of bee venom in cancer: recent trends and developments
Published in Toxin Reviews, 2022
Ayşegül Varol, Serap Sezen, Dilhan Evcimen, Atefeh Zarepour, Gönül Ulus, Ali Zarrabi, Gamal Badr, Sevgi Durna Daştan, Asya Gülistan Orbayoğlu, Zeliha Selamoğlu, Mehmet Varol
Melittin, which is a very major polypeptide with 26 amino acid residues and a molecular weight of 2850 Da, is known as the main and most important component of bee venom (near 40–60% of its dry weight) and shows many biological activities including but not limited to the anti-inflammatory, anti-oxidant, and anti-apoptotic effects (Table 1) (Kim et al. 2021). It is a cationic amphipathic polypeptide that can enhance the action of phospholipase A2, and can be incorporated into both natural and synthetic phospholipid bilayers and exerts diverse effects on living cells (Raghuraman and Chattopadhyay 2007). In addition to its effects on the metabolic functions of mammalian cells, it exerts cytotoxic effects on intestinal cells as well as on hematopoietic cells, thymocytes, erythrocytes and lymphocytes (Gajski and Garaj-Vrhovac 2011). On the other hand, it has been reported that melittin rehabilitates fibrosis and kidney damage after unilateral ureteral obstruction in mice (An et al. 2016).
Antimicrobial peptides and other peptide-like therapeutics as promising candidates to combat SARS-CoV-2
Published in Expert Review of Anti-infective Therapy, 2021
Masoumeh Sadat Mousavi Maleki, Mosayeb Rostamian, Hamid Madanchi
The pore-forming peptides, like Melittin, represent a subset of AMPs that binds to the virus coating and forms a channel-like structure or pore in two lipid bilayers [25]. To date, no studies have been performed on the efficacy of Melittin or its derivatives on SARS-CoV-2. However, in a study in China, bee venom was effective in preventing COVID-19 in beekeepers exposed to bee stings [74]. In this study, apitherapy in 121 people prevented them from developing COVID-19, while three of them were in close contact with COVID-19 patients [74]. Apitherapy is a branch of alternative medicine that uses honey bee products, including honey, pollen, propolis, royal jelly, and bee venom [75]. Regarding previous research on the antiviral role of Melittin and its immunomodulatory function, it can be suspected that in their study the most important effective component in bee venom has been Melittin.