Abstract:
© 2014 Pleiades Publishing, Ltd. 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.