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In present paper, molecular dynamics is used to study amyloid fibril destruction by oppositely charged dendrimers. Dendrimers are often used for delivery of drugs and biological molecules. They also could be used as antibacterial, antiviral and antiamyloid agents. Since lysine dendrimers are less toxic than conventional synthetic dendrimers), we chose them and studied system consisting of 3rd generation dendrimers and stack of 16 short amyloid peptides in water. It was shown that lysine dendrimer destroys amyloid stack and forms stable complex with amyloid peptides. We investigated the structures of the complex in equilibrium state and obtained that peptides in complex stay mainly on the surface of dendrimer and do not penetrate into it. The data can be used in future in treatment of Alzheimer's disease, since it is believed that one of the reasons for its occurrence is the formation of amyloid fibrils.