Protein biochips based on macroporous polymer supports: Material properties and analytical potential.

A series of rigid macroporous polymer layers differed by hydrophobic-hydrophilic properties was synthesized in situ in preliminary fabricated wells and applied as the platforms for protein biochips. Scanning electron microscopy, etalon porosimetry and BET analysis were used for materials characterization. The comparison of analytical efficiency of the developed platforms allowed for the choice of the most optimal polymer, as well as the evaluation of impact of material porous properties.

Amphiphilic polypeptides with prolonged enzymatic stability for the preparation of self-assembled nanobiomaterials.

Due to their excellent biocompatibility and biodegradability, polypeptides have emerged as versatile bio-inspired scaffolds for the preparation of artificial biomaterials. In order to create self-assembled polypeptide nanoparticles with enhanced stability towards enzymatic degradation, we synthesized a series of random and block polypeptides based on lysine and α-aminoisobutyric acid (Aib) by the ring-opening polymerization of N-carboxyanhydrides (ROP NCA) of the corresponding amino acids. A conformational analysis carried out by means of FT-IR absorption and CD spectroscopies revealed a noticeable difference between random and block copolymers.

Immobilized enzyme reactors based on monoliths: Effect of pore size and enzyme loading on biocatalytic process.

Macroporous monolithic columns with different mean pore size (from 360 to 2020 nm) and appropriate flow-through properties were synthesized using free radical in situ copolymerization of glycidyl methacrylate, 2-hydroxyethyl methacrylate and ethylene dimethacrylate. In order to predict the composition of porogen mixture to generate the pores in the interested size interval, the Hildebrand theory was used. Ribonuclease A and its specific low- and macromolecular substrates cytidine-2',3'-cyclic monophosphate sodium salt and RNA were applied as model system.

Self-assembled polypeptide nanoparticles for intracellular irinotecan delivery.

In this research poly(l-lysine)-b-poly(l-leucine) (PLys-b-PLeu) polymersomes were developed. It was shown that the size of nanoparticles depended on pH of self-assembly process and varied from 180 to 650nm. The biodegradation of PLys-b-PLeu nanoparticles was evaluated using in vitro polypeptide hydrolysis in two model enzymatic systems, as well as in human blood plasma.

Macroporous monoliths for biodegradation study of polymer particles considered as drug delivery systems.

Nanostructures based on biodegradable polymers are often considered as drug delivery systems. The properties of these nanomaterails towards in vitro biodegradation are very important and usually are studied using the model physiological conditions. In this work the novel approach based on application of monolithic immobilized enzyme reactors (IMERs) as the systems for biodegradation study of the nanoobjects of different nature and morphology was suggested.