Self-Assembling Systems Based on Amphiphilic Poly-N-vinylpyrrolidone and Their Interaction with Model Proteins

A. L. Villemson¹, E. V. Malykh¹, M. I. Shtilman², and N. I. Larionova^1*

¹School of Chemistry, Lomonosov Moscow State University, Moscow 119992, Russia; fax: (095) 939-5417; E-mail: nilar@enzyme.chem.msu.ru

²Mendeleev University of Chemical Technology, Miusskaya pl. 9, Moscow 125047, Russia

^* To whom correspondence should be addressed.

Received June 3, 2002; Revision received June 26, 2002

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Polymeric particles formed by stearoyl-poly-N-vinylpyrrolidone (PVP-stear) of M_n = 2600 were obtained in aqueous solution, and their shape and size distribution were characterized. The size of the particles was shown to decrease with an increase in the ionic strength of the solution. Interaction of PVP-stear and its aggregates with model proteins (Bowman-Birk soybean proteinase inhibitor (BBI) and its hydrophobized derivatives) was studied. The possibility of inclusion of both native BBI and oleoylic derivative of BBI in the PVP-stear polymeric aggregates was investigated. It was established that polymeric particles with a diameter of 30 nm formed under certain concentration ratios between PVP-stear and poorly soluble dioleoyl BBI are capable of solubilization of dioleoyl BBI as well as prevention of its inactivation at low pH values.

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KEY WORDS: self-assembling systems, colloidal particles, polymeric aggregates, stearoyl-poly-N-vinylpyrrolidone, Bowman-Birk soybean proteinase inhibitor

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