Results 171 to 180 of about 10,158 (214)
Study of vesicle leakage induced by melittin
Biochimica Et Biophysica Acta - Biomembranes, 1995 The leakage induced by melittin, a membrane-perturbing amphipathic peptide, from large unilamellar 1-palmitoyl-2-oleoylphosphatidylcholine (POPC) vesicles was studied using calcein as fluorescent marker.
Michel Lafleur
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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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The interaction of calmodulin with melittin
Biochemical and Biophysical Research Communications, 1986Studies utilizing the interaction of melittin with the 1-106 fragment of calmodulin, the protection of calmodulin from tryptic digestion by melittin, and the interaction of the carbocyanine dye Stains-all with the calmodulin-melittin complex have indicated that complex formation of calmodulin with melittin involves the alpha-helical connecting bridge ...
C G, Caday, R F, Steiner
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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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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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Interactions of 2,2,2‐trifluoroethanol with melittin
Magnetic Resonance in Chemistry, 2009AbstractMelittin dissolved in 42% trifluoroethanol‐water at pH 2 has been shown to be α‐helical between residues 6 and 12 and between residues 13 and 25, with the two helical regions separated by a bend at the Leu13 residue. The inter‐helix angle was found to be 154 ± 3° at 0 °C and 135 ± 3° at 25 °C.
Robert C, Neuman, John T, Gerig
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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 ...
Curcio-Vonlanthen V +4 more
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The actions of melittin on membranes
Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1990The molecular mechanisms underlying the various effects of melittin on membranes have not been completely defined and much of the evidence described indicates that different molecular mechanisms may underlie different actions of the peptide. Ideas about the formation of transbilayer aggregates of melittin under the influence of a transbilayer potential,
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Characterization of Melittin Effects in Synaptosomes
Neurochemical Research, 1997The effects of melittin at increasing concentrations on: [3H]GABA release from mouse brain synaptosomes; on the radioactivity released from [3H]arachidonic acid labeled synaptosomal membranes; on synaptosomes ultrastructure and on the leakage of the cytoplasmic marker, lactate-dehydrogenase (LDH) was investigated.
L, González +3 more
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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, D C Tosteson, Tosteson D C
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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, D C Tosteson, Tosteson D C
exaly +3 more sources