There is currently no engineering material used in cardiovascular implants and devices that completely prevents blood clotting when in long-term contact with flowing whole blood. Considering implantable biomaterials and devices, adsorption of nonspecific proteins, such as albumin, fibrinogen, and von Willebrand factor, can be a particularly undesirable event, which can lead to biological responses such as coagulation, thrombosis, and bacterial infection.<br/>The dominant approach to developing next-generation blood-compatible surfaces is to design surface chemistries and structures that reduce or eliminate protein adsorption to prevent blood clotting. This work proposes a new paradigm for developing blood-contacting surfaces by strategically mimicking key features of the inside surfaces of blood vessels: negatively charged glycosaminoglycans organized into a polymer brush with nanoscale domains. The interactions of blood proteins with glycocalyx mimics are revealed in detail using single-molecule video microscopy. This novel approach shows for the first time that the nanoscale structure and organization of glycosaminoglycans in the glycocalyx is essential to (i) reduce protein adsorption, (ii) reversibly bind fibrinogen, and (iii) suppress fibrin polymerization. This work reveals a previously unknown mechanism whereby the endothelial glycocalyx prevents blood clotting that can be exploited for the design of blood-compatible materials.<br/>

Blood protein interaction with nanostructured glycocalyx mimetic surfaces

256th National Meeting (2018)

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