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Melittin is a water-soluble toxic peptide derived from the venom of the bee. Although many studies show the anti-tumor activity of melittin in human cancer including glioma cells, the underlying mechanisms remain elusive.
Hui Zhang +5 more
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The Structure of a Melittin-Stabilized Pore [PDF]
Melittin has been reported to form toroidal pores under certain conditions, but the atomic-resolution structure of these pores is unknown. A 9-μs all-atom molecular-dynamics simulation starting from a closely packed transmembrane melittin tetramer in DMPC shows formation of a toroidal pore after 1 μs.
Leveritt, John M. +2 more
openaire +2 more sources
Comparative Determination of Melittin by Capillary Electrophoretic Methods
Bee venom from honey bees (Apis Mellifera L.) is known to have many pharmacological and biological properties. Melittin, a peptide consisting of 26 amino acids, is known as the main component of bee venom.
Melda AKAY +3 more
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Conformational changes in melittin upon complexation with an anionic melittin analog
Melittin and its Glu‐(7,21,22,23,24) analog upon mixing in equimolar concentrations form a hybrid oligomer with significant helical structure, in conditions in which each peptide separately adopts a largely disordered structure. The hybrid exhibits both cold‐ and heat‐induced denaturations similar to the phenomena exhibited by proteins. The hybrid also
Ramalingam, Kalaiyarasi +2 more
openaire +2 more sources
Background Melittin is one of the most studied antimicrobial peptides, and several in vitro experiments have demonstrated its antibacterial efficacy. However, there is evidence showing melittin has non-promising effects such as cytotoxicity and hemolysis.
Parvin Askari +3 more
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Melittin based nano drug delivery system for cancer therapy
Melittin is a 26 amino acid polypeptide with a wide range of toxicological and pharmacological effect. It constitutes 40%-60% of dry honeybee (Apis melifera) venom.
Semanti Ghosh, Smarta Das
core +1 more source
Structural studies of bee melittin
The question of how proteins refold in passing from an aqueous phase to an amphipathic environment such as a membrane is beig addressed by a structural study of bee melittin. Melittin is the toxic, main protein of bee venom, and has been shown by others to integrate into natural and synthetic membranes and to lyse a variety of cells.
Eisenberg, David +2 more
openaire +2 more sources
Antimicrobial peptides (AMPs) are naturally occurring entities with potential as pharmaceutical candidates and/or food additives. They are present in many organisms including bacteria, insects, fish and mammals.
O\u27Brien, Peter J. +12 more
core +1 more source
Melittin is a major peptide component of sweet bee venom that possesses anti-allergic, anti-inflammatory, anti-arthritis, anti-cancer, and neuroprotective properties. However, the therapeutic effects of melittin on muscle injury have not been elucidated.
Jae Eun Lee +4 more
doaj +1 more source
Asian honeybee venom is widely used in traditional oriental medicine. Melittin is the main component of Asian honeybee venom. In the present study, an ultra-performance liquid chromatography-quadrupole time-of-flight mass spectrometry (UPLC-QqTOF-MS ...
Sheng Huang +4 more
doaj +1 more source

