Results 31 to 40 of about 7,897 (182)
BMC Pharmacology and Toxicology, 2021 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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Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue
Biophysical Journal, 1982 The cytotoxic peptide from honeybee venom, melittin, and a synthetic peptide analogue of it lyse human erythrocytes in a biphasic process. The kinetics of the lysis in 0.30 M sucrose, 0.01 M sodium phosphate, pH 7.30 at 4 degrees C were investigated. Our results show that melittin rapidly binds to the outer surface of the erythrocyte membrane, and the ...
DeGrado, W.F. +4 more
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Journal of Apicultural Science, 2015 Two enzyme-linked immunosorbent assay (ELISA) - based detection systems: indirect competitive ELISA and biotinylated double antibody sandwich ELISA (DAS-ELISA) were developed to determine the melittin concentration in honeybee (Apis mellifera) venom and ...
Suh Lindsey Y. K. +5 more
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Molecules, 2019 Malignant melanoma is the deadliest form of skin cancer and highly chemoresistant. Melittin, an amphiphilic peptide containing 26 amino acid residues, is the major active ingredient from bee venom (BV).
Haet Nim Lim +2 more
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Structural Dynamics, 2015 Trifluoroacetic acid (TFA) may be the cause of the bottleneck in high resolution structure determination for protein-peptide complexes. Fragment based drug design often involves the use of synthetic peptides which contain TFA (excipient). Our goal was to explore the effects of this excipient on a model complex: centrin-melittin-TFA.
Pastrana Rios, Belinda +2 more
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Structural studies of bee melittin
Biophysical Journal, 1980 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
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Journal of Pharmacological Sciences, 2019 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
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Effect of Melittin on Metabolomic Profile and Cytokine Production in PMA-Differentiated THP-1 Cells
Vaccines, 2018 Melittin, the major active peptide of honeybee venom (BV), has potential for use in adjuvant immunotherapy. The immune system response to different stimuli depends on the secretion of different metabolites from macrophages.
Abdulmalik M. Alqarni +4 more
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Ultrastructural observation on sterilization of melittin [PDF]
Science China Life Sciences, 2011 ABSTACT: The effects of melittin on growth and bacteriostasis of four pathogens were extensively investigated using scanning electron microscopy (SEM) and transmission electron microscopy (TEM). The results indicated that the melittin had a marked bacteriostatic effect on the four pathogenic bacteria. Among these, E.
Wang, GuanLin +4 more
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Toxins, 2020 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
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