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000448258 1001_ $$0P:(DE-HGF)0$$aChernysheva, Maria G.$$b0$$eCorresponding author
000448258 245__ $$aStructural peculiarities of lysozyme – PLURONIC complexes at the aqueous-air and liquid-liquid interfaces and in the bulk of aqueous solution
000448258 260__ $$aNew York, NY [u.a.]$$bElsevier$$c2020
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000448258 520__ $$aInteraction between proteins and synthetic polymers that represent a perspective potential in drug delivery or/and already used in medicine plays a key role in biological functioning of both molecules along with a system as a whole. In present study association between hen egg white lysozyme and Pluronic triblock-copolymers (L121, P123 and F127) in the bulk of the solution as well as at the aqueous-air and liquid-liquid interfaces was analyzed by means of spectroscopic and radiochemical assay. In protein-Pluronic complexes lysozyme keeps the secondary structure (CD and SAXS data results), while fluorescence and UV-analysis indicates changes in the local surrounding of fluorophoric amino acid residues. Radiochemical assay in combination with molecular docking reveals the formation of the complexes, in which proline residues turned to the interface between water and hydrophobic medium.
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000448258 7001_ $$0P:(DE-HGF)0$$aShnitko, Alexey V.$$b1
000448258 7001_ $$0P:(DE-HGF)0$$aKsenofontov, Alexander L.$$b2
000448258 7001_ $$0P:(DE-HGF)0$$aArutyunyan, Alexander M.$$b3
000448258 7001_ $$0P:(DE-HGF)0$$aPetoukhov, Maxim V.$$b4
000448258 7001_ $$0P:(DE-HGF)0$$aBadun, Gennadii A.$$b5
000448258 773__ $$0PERI:(DE-600)1483284-7$$a10.1016/j.ijbiomac.2020.04.221$$gVol. 158, p. 721 - 731$$p721 - 731$$tInternational journal of biological macromolecules$$v158$$x0141-8130$$y2020
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