Abstract
The structure and properties of supramolecular complexes of α-chymotrypsin with hydroxyl-containing alkyl ammonium gemini surfactants (GSs) — α,ω-alkanedyl-bis(hydroxyethylmethylcetyl ammonium dibromides), with a polymethylene spacer of varying length have been studied. IR spectroscopy and tryptophan fluorescence data show that the interaction of GSs with α-chymotrypsin leads to changes of different intensity in the structural state of proteins. The most probable complexation mode of enzyme with GSs have been proposed by the molecular docking method. A correlation is found between the activity of α-chymotrypsin and the length of the GS spacer moiety. The enzyme activity correlates with the change in the substrate concentration in the aqueous phase of the surfactant micellar solution.
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Original Russian Text © 2014 Yu. A. Valiullina, E. A. Ermakova, D. A. Faizullin, A. B. Mirgorodskaya, Yu. F. Zuev.
Zhurnal Strukturnoi Khimii, Vol. 55, Supplement 2, pp. S375–S382, 2014.
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Valiullina, Y.A., Ermakova, E.A., Faizullin, D.A. et al. Structure and properties of complexes of α-chymotrypsin with hydroxyl-containing gemini dicationic surfactants with a spacer moiety of varying length. J Struct Chem 55, 1556–1564 (2014). https://doi.org/10.1134/S0022476614080253
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DOI: https://doi.org/10.1134/S0022476614080253