Blood-material interactions are critical for the performance and biocompatibility of implantable medical devices used in thousands of patients everyday. When a biomaterial is introduced into the body, protein adsorption and activation of complement proteins occur. Complement proteins are mediators of inflammation, and are therefore of interest in biomaterials research. Success often depend on interactions between the biomaterial’s surface and its physiological environment. Modifications are often made to the surface of biomaterials to modulate their physical and chemical properties in order to improve the functionality of the biomaterial in a given application.
When a biomaterial or medical device is placed in the body proteins almost immediately start to adsorb to the surface. In some cases, such as orthopedic implants, this is beneficial because the proteins can facilitate the attachment of cells that will lead to proper integration of the device. In other cases, for example with stents, the rapid adsorption of plasma proteins, followed by platelet adhesion and activation causes thrombus formation. Key factors in clot formation are the chemical and physical nature of the surfaces and their interactions with the blood components.
The QCM-D technology enables real-time analysis of protein adsorption onto a variety of surfaces. Specifically, the amount of protein bound as well as the rate of adsorption can be analyzed. QCM-D can be a useful tool in evaluating the immunogenicity of different biomaterials.
Read more about how surface-induced complement activation can be analyzed with QCM-D in our application note:
Proteins tend to passively adsorb to surfaces. The amount adsorbed depends on many factors such as the protein itself, the ambient conditions and the surface material. So how can the adsorbed amount at these various conditions be assessed? Here we show how protein adsorption can be quickly measured.
Proteins are vital for life and perform a wide range of essential biochemical tasks in all living organisms. It is important that the proteins are correctly folded and functional. However, sometimes the control mechanisms fail and accumulated aggregates transform into protein megastructures.