ИСТИНА

The 4th generation pyridylphenylene dendrimers with fully pyridine-based periphery were synthesized, and their ability to form nanofilms with different proteins was investigated in the present work. For model proteins such as dairy beta and kappa-caseins, alpha-lactalbumin, recombinant sheep prion and lysozyme, the ability to integrate into 400-700 nm thick films was found. Protein incorporation into the nanofilms was confirmed by SDS-PAGE of the solution remaining after the incubation with the dendrimer and the formation of nanofilms (no protein was found in the supernatant). Protein/dendrimer ratio was discovered to play crucial role in the formation of nanofilms. Structure of thus obtained nanofilms was investigated using light and atomic force microscopy. The obtained nanostructures were analyzed for stability, resistance to pH changes and the action of detergents. We have also conducted in silico molecular modeling of the self-organization of cationic pyridylphenylene dendrimers with proteins into regular nanostructures and proposed a possible model of spatial organization of molecules. We attempted to model the structure of the G4 dendrimer complex with lysozyme as a model object. We believe that the obtained dendrimer-protein systems are promising as means for developing new biomaterials, medical systems and highly stable biosensors.