Biophysics, Poster

LUMINESCCENT PROBES IN DETERMINATION OF THE STRUCTURAL CHANGES IN PROTEINS, WHICH CONTAIN SALTS OF HEAVY METALS.

Andrey Melnikov, Saratov State Technical University, Russia
Ekaterina Naumova, Saratov State Technical University, Russia

ABSTRACT

We studied the quenching of the electronic-excited states of polar and nonpolar luminescent probes bound to proteins, during their structural rearrangement, by salts of heavy metals. Using the method of the probe phosphorescence quenching, we determined peculiarities of the quenching of the excited states of polycyclic aromatic hydrocarbons and luminescent probes from xanthenes row bound to human serum albumin, during the process of its structural changes, by thallium, plumbum and cesium ions. Structural changes in proteins were stimulated by addition of surfactant - sodium dodecylsulfate. The conducted investigations made it possible to establish the dependence of rate constant of quenching of triplet states of eosin molecules on the concentration of SDS in the solution. It is supposed that this dependence is connected with protein denaturation under SDS action. Processes of quenching of excited states of some PAHs: anthracene, pyrene, 1,2 benzanthracene by ions of plumbum, thallium, iodine. It is established, that vibronic structure of pyrene fluorescence spectra is not sensitivity to presence of heavy metals. Increase of the concentration of heavy metals leads to protein denaturation, which is observed by change in the polarity index of pyrene and by decrease of lifetime of triplet states of luminescent probes.

Representing author

photo

Mr. Andrei Gennadyevich Melnikov

Saratov State University, Assistant
Saratov, Russia

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