Melittin is a major toxic component of bee venom (Apis mellifera). It is not known whether melittin is involved in bone metabolism and osteoclastogenesis. The aim of this study was to determine the role of melittin in the regulation of osteoclastogenesis. In vitro osteoclastogenesis assays were performed using mouse RAW 264.7 cells and bone marrow-derived macrophages (BMMs) treated with recepto...

Understanding the molecular mechanism of the interaction of amphipathic and antimicrobial peptides with membranes is of fundamental interest, especially because of the potential of amphipathic peptides as therapeutics. The most studied amphipathic peptides in this context are certainly melittin, magainin and alamethicin, of which melittin is the only one to exhibit a powerful hemolytic and ther...

The cytolytic activity of the bee venom toxin, melittin, is abolished on permethylation of the ammonium groups into quaternary trimethylammonium groups. The loss of activity in permethylated melittin may result partly from the absence of the hydrogen bonding potential and partly from steric effects involving the bulky trimethylammonium groups. Displacing the trimethylammonium groups away from t...

Antimicrobial peptides are effectors of innate immunity, providing their hosts with rapid non-specific defence against parasitic invaders. In this report, the effects are assessed of two well-characterized antimicrobial amphipathic peptides (melittin and cecropin) on human immunodeficiency virus 1 (HIV-1) replication and gene expression in acutely infected cells at subtoxic concentrations. Prod...

Vascular endothelial growth factor and its tyrosine kinase receptors have been identified as key mediators of the regulation of pathologic blood vessel growth and maintenance in the promotion of angiogenesis and tumor growth. Therefore, an alternative approach to destroying tumor endothelium would be to make this tissue particularly sensitive to VEGF-mediated drug delivery. To verify this hypot...

Inflammation is a pervasive phenomenon triggered by the innate and adaptive immune systems to maintain homeostasis. The phenomenon normally leads to recovery from infection and healing, but when not properly phased, inflammation may cause immune disorders. Bee venom is a toxin that bees use for their protection from enemies. However, for centuries it has been used in the Orient as an anti-infla...

The widespread distribution of cationic antimicrobial peptides capable of membrane fragmentation in nature underlines their importance to living organisms. In the present work, we determined the impact of the electrostatic interactions associated with the cationic C-terminal segment of melittin, a 26-amino acid peptide from bee venom (net charge +6), on its binding to model membranes and on the...

Calmodulin serves as a calcium-dependent regulator in many metabolic pathways and is known to bind with high affinity to various target proteins and peptides. One such target is the small peptide melittin, the principal component of honeybee venom. The calmodulin-melittin system was used as a model system to gain further insight into target recognition of calmodulin. Using chemical cross-linkin...

Although potent, proteins often require chemical modification for therapeutic use. Immunogenicity, difficult synthesis, and scale-up of these modifications are all engineering obstacles that stand in the way of expanding the use of these therapeutics. Melittin, a peptide derived from bee venom, has been shown to modulate inflammation. Although potentially therapeutic, the native peptide causes ...

Melittin is the principal protein component of bee venom and is believed to function as a lytic agent. In aqueous salt solution, it is a tetramer of identical peptides, each with 26 amino acid residues. Although its amino acid composition is unusually nonpolar, and although it is believed to integrate into membranes while lysing cells, melittin is water-soluble at neutral pH. Two crystal forms ...