The bee venom, used in treatment of inflammatory and articular diseases, is a complex mixture of peptides and enzymes and the presence of tryptophan allows the investigation by fluorescence techniques. Steady state and time-resolved fluorescence spectroscopy were used to study the interaction between bee venom extracted from Apis mellifera and three micro heterogeneous systems: sodium dodecylsulphate (SDS) micelles, sodium dodecylsulphate-poly(ethylene oxide) (SDS-PEO) aggregates, and the polymeric micelles LUTROL F127, formed by poly(ethylene oxide)-poly(propylene oxide)- poly(ethylene oxide). Fluorescence parameters in buffer solution were typical of peptides containing tryptophan exposed to the aqueous medium, and they gradually changed upon the addition of surfactant and polymeric micelles, demonstrating the interaction of the peptides with the micro heterogeneous systems. Quenching experiments were carried out using the N-alkylpyridinium ions (ethyl, hexyl, and dodecyl) as quenchers. In buffer solution the quenching has low efficiency and is independent of the alkyl chain length of the quencher. In the presence of the micro heterogeneous systems the extent of static and dynamic quenching enhanced, showing that both fluorophore and quenchers reside in the microvolume of the aggregates. The more hydrophobic quencher (dodecyl pyridinium ion) provides higher values for K (SV) and dynamic quenching constants, and SDS-PEO aggregates are most efficient to promote interaction between peptides and alkyl pyridinium ions. The results proved that bee venom interacts with drug delivery micelles of the copolymer LUTROL F127.
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http://dx.doi.org/10.1007/s10895-006-0077-9 | DOI Listing |
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