Results 171 to 180 of about 11,509 (217)

Melittin-phospholipid interaction Evidence for melittin aggregation

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1981
Abstract 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, M, Thompson, A K, Mukhopadhyay   +2 more
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The interaction of calmodulin with melittin

Biochemical and Biophysical Research Communications, 1986
Studies 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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Melittin and Cancer

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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Peptide inhibitors of melittin action

Journal of Protein Chemistry, 1996
The 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, J, Werkmeister, A, Kirkpatrick, C, Curtain, G, Pantela, D E, Rivett   +5 more
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The actions of melittin on membranes

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1990
The 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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Picosecond fluorescence spectrochronography of protein melittin and melittin-membrane complexes

Journal of Molecular Structure, 1990
Abstract 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, A.S. Ladokhin, N.V. Lebedeva, B.N. Toleutaev   +3 more
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Interactions of 2,2,2‐trifluoroethanol with melittin

Magnetic Resonance in Chemistry, 2009
AbstractMelittin 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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Melittin: An allergen of honeybee venom

Journal of Allergy and Clinical Immunology, 1977
The presence of serum IgE antibodies to melittin was tested by the radioallergosorbent test (RAST). Melittin, the principal protein of honeybee venom, was isolated by gel filtration on Sephadex G-75 and covalently bound to cyanogen bromide-activated microcrystalline cellulose.
B R, Paull, J W, Yunginger, G J, Gleich
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Melittin-regenerated purple membrane

Biochemistry (Moscow), 2009
We 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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Melittin lysis of red cells

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, S J, Holmes, M, Razin, D C, Tosteson   +3 more
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