Several amphipathic and cationic substances are known to bind lipid A, the toxic component of bacterial lipopolysaccharides. In this report, we have characterized, by fluorescence methods, the interaction of melittin, an amphipathic and basic 26-residue polypeptide isolated from bee venom, with lipid A. The stoichiometry of the complex appears to be two molecules of melittin to one of lipid A w...

Melittin, the principal constituent in bee venom, is an attractive candidate for cancer therapy. However, its clinical applications are limited by hemolysis, nonspecific cytotoxicity, and rapid metabolism. Herein, a novel genetically engineered vesicular antibody-melittin (VAM) drug delivery platform was proposed validated targeted combination VAM generated from cellular plasma membrane bio-syn...

To study mechanisms whereby lytic proteins disrupt biomembranes, artificial phospholipid spherules (liposomes) were exposed to melittin, a cationic peptide in which sequences of hydrophobic (Positions 1 to 20) and hydrophilic (Positions 21 to 26) amino acids are unequally distributed. At concentrations above 1OF M, melittin, which is the major toxin of bee venom, released marker anions (CrOb) o...

Tumor invasion and metastasis are the critical steps in determining the aggressive phenotype of human cancers. Melittin, a major component of bee venom, has been reported to induce apoptosis in several cancer cells. However, the mechanisms of melittin involvement in cancer invasion and metastasis remain unclear. Our previous study indicated that melittin inhibits cyclophilin A (CypA), a ubiquit...

BACKGROUND It has been previously reported that melittin, the main ingredient of honey bee venom, has anticancer properties. However, there appears to be no earlier study focusing on the isolation of melittin from Iranian honey bee venom (Apis mellifera meda), and evaluation of its effect on cancerous cells. METHODS We isolated melittin using reversed-phase high performance liquid chromatogra...

Background . Melittin is a major constituent of honeybee venom and comprises water-soluble surfactant peptide with cytolytic effects potentially applicable in anticancer therapy. We evaluated the impact melittin from Bashkir ( Apis mellifera L.) on cell viability various prostate cancer lineages. Materials methods. MTT assays index estimation were used to evaluate effect proliferation various-g...

Melittin, a membrane-active peptide with antimicrobial activity, was investigated at the interface formed between two immiscible electrolyte solutions (ITIES) supported on a metallic electrode. Ion-transfer voltammetry showed well-defined semi-reversible transfer peaks along with adsorptive peaks. The reversible adsorption of melittin at the liquid-liquid interface is qualitatively discussed fr...

Clinical application of antimicrobial peptides (AMPs), as with conventional antibiotics, may be compromised by the development of bacterial resistance. This study investigated AMP resistance in methicillin resistant Staphylococcus aureus, including aspects related to the resilience of the resistant bacteria toward the peptides, the stability of resistance when selection pressures are removed, a...

Abstract Melittin, the most potent pharmacological ingredient of honey bee venom, induces haemolysis, lymphocyte lysis, long-term pain, localised inflammation, and hyperalgesia. In this study, efforts were made to subdue melittin’s ill effects using a chaperone peptide called ‘mini-αA-crystallin’ (MAC) derived from eye lens αA-crystallin. Haemolytic test on human red blood cells, percentage via...

Melittin, which acts as a membrane-disrupting lytic peptide, is not only cytotoxic to tumors, but also vital to normal cells. Melittin had low toxicity when coupled with target peptides. Despite significant research development with the fused toxin, a new fused toxin is needed which has a cleavable linker such that the fused toxin can release melittin after protease cleavage on the tumor cell s...