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A Clinical Study for the Development of a Bee Venom Allergy Diagnostic Kit. [PDF]
Yu JS +5 more
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Melittin inhibits proliferation, migration, and invasion in osteosarcoma cell lines using 2D and 3D models. [PDF]
Pedro G +4 more
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Melittin-phospholipid interaction Evidence for melittin aggregation
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1981Abstract The fluorescence spectra of the single tryptophan residue of melittin in 0.15 M potassium phosphate solution and when bound to egg phosphatidylcholine bilayer liposomes practically coincide and exhibit a large blue shift relative to that in aqueous solution.
S, Georghiou +2 more
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Melittin-regenerated purple membrane
Biochemistry (Moscow), 2009We have investigated the character of melittin-regenerated purple membrane. Adding melittin to blue membrane causes the color transition and partial regeneration of the photocycle and the proton pump. The reconstitution of bacteriorhodopsin by melittin is proved to be charge-dependent.
Yue, Zhang, Tao, Su, Kun-Sheng, Hu
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Journal of Apitherapy, 2016
Cancer no longer is the automatic death sentence of centuries past, yet it remains a leading cause of global morbidity and mortality despite advances in detection, treatment, and survival in the field of oncology. The search for natural chemotherapeutic substances has accelerated research into the use of venom as a potential weapon against cancer.
Anna Tacn, PhD PhD
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Cancer no longer is the automatic death sentence of centuries past, yet it remains a leading cause of global morbidity and mortality despite advances in detection, treatment, and survival in the field of oncology. The search for natural chemotherapeutic substances has accelerated research into the use of venom as a potential weapon against cancer.
Anna Tacn, PhD PhD
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Molecular parameters in melittin immunogenicity
Journal of Peptide Science, 1997Based on immunogenicity studies, two T-cell epitopes in melittin were found to be functional in guinea pigs, one being centrally located, the other one residing in the C-terminal chain. In Balb/c mice only the central epitope was found to be active. A human T-cell clone was found by T-cell proliferation studies to employ strictly the C-terminal chain ...
V, Curcio-Vonlanthen +4 more
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Picosecond fluorescence spectrochronography of protein melittin and melittin-membrane complexes
Journal of Molecular Structure, 1990Abstract The results are presented of the study of protein melittin structure and dynamics when incorporated into the phospholipid bilayer carried out by time-resolved fluorescence spectroscopy with laser UV ps-pulse excitation.
A.Yu. Chikishev +3 more
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Peptide inhibitors of melittin action
Journal of Protein Chemistry, 1996The sequence of peptides necessary to inhibit melittin-induced lysis was studied using 13 peptide analogues of the inhibitor Ac-IVIFDC-NH2. Although this inhibitor is a disulfide-linked dimer, inhibition was equally effective if the thiol SH was blocked or replaced by methionine or lysine.
D, Hewish +5 more
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Membrane matrix disruption by melittin
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1972Abstract Electron spin resonance spectroscopy was used to examine the interaction of the lytic polypeptide, melittin, with model membrane systems in order to determine the physical basis for its alterations of membrane properties. Sonically dispersed egg lecithin (phosphatidylcholine), phosphatidylserine, extracted Escherichia coli phospholipids, and
J C, Williams, R M, Bell
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The Journal of Membrane Biology, 1985
This paper describes experiments designed to explore interactions between human red blood cell membranes and melittin, the main component of bee venom. We found that melittin binds to human red cell membranes suspended in isotonic NaCl at room temperature, with an apparent dissociation constant of 3 X 10(-8) M and maximum binding capacity of 1.8 X 10(7)
M T, Tosteson +3 more
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This paper describes experiments designed to explore interactions between human red blood cell membranes and melittin, the main component of bee venom. We found that melittin binds to human red cell membranes suspended in isotonic NaCl at room temperature, with an apparent dissociation constant of 3 X 10(-8) M and maximum binding capacity of 1.8 X 10(7)
M T, Tosteson +3 more
openaire +2 more sources

