Binding of poly(amidoamine), carbosilane, phosphorus and hybrid dendrimers to thrombin—Constants and mechanisms
Dzmitry Shcharbin, Elzbieta Pedziwiatr-Werbicka, Aliaksandra Vcherashniaya, Anna Janaszewska, Monika Marcinkowska, Piotr Goska, Barbara Klajnert-Maculewicz, Maksim Ionov, Viktar Abashkin, Aliaksei Ihnatsyeu-Kachan, F. Javier de la Mata, Paola Ortega, Rafael Gomez-Ramirez, Jean-Pierre Majoral, Maria Bryszewska
Colloids and Surfaces B: Biointerfaces
Thrombin is an essential part of the blood coagulation system; it is a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, and catalyzes many other coagulation-related reactions. Absorption at its surface of small nanoparticles can completely change the biological properties of thrombin. We have analyzed the influence on thrombin of 3 different kinds of small nanoparticles: dendrimers (phosphorus-based, carbosilane based and polyamidoamine) and 2 hybrid systems containing carbosilane, viologen and phosphorus dendritic scaffolds in one single molecule, bearing different flexibility, size and surface charge. There was significant alteration in the rigidity of the rigid dendrimers in contrast to flexible dendrimers. These differences in their action are important in understanding interactions taking place at a bio-nanointerface.
Circular dichroism, Secondary structure, Chemical stability, Nanostructures, Biochemistry, Materials