Binding of poly(amidoamine), carbosilane, phosphorus and hybrid dendrimers to thrombin—Constants and mechanisms

July 28, 2017

Title

Binding of poly(amidoamine), carbosilane, phosphorus and hybrid dendrimers to thrombin—Constants and mechanisms

Author

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

Year

2017

Journal

Colloids and Surfaces B: Biointerfaces

Abstract

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.

Instrument

J-815

Keywords

Circular dichroism, Secondary structure, Chemical stability, Nanostructures, Biochemistry, Materials