Chapter 6: Fibrous Proteins Interactions with Modified Surfaces of Biomaterials
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Published:02 Nov 2011
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Special Collection: 2011 ebook collection , 2011 ebook collection , 2011-2015 materials and nanoscience subject collectionSeries: Nanoscience & Nanotechnology
C. Wolf-Brandstetter and D. Scharnweber, in Biological Interactions with Surface Charge in Biomaterials, ed. S. Tofail, The Royal Society of Chemistry, 2011, ch. 6, pp. 75-89.
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Fibrous proteins (or scleroproteins) provide the structural integrity of several tissues due to their unique secondary structure and form the main components of the so-called extracellular matrix (ECM). The ECM is an important factor that regulates cell behaviour. Hence the utilization of ECM components for biomaterial coatings has become a focus of interest. In the majority of applications, collagen is the material of choice due to its predominant occurrence in extracellular tissues such as bone and cartilage. Collagen can be modified using a number of different glycoproteins, proteoglycans and glycosaminoglycans, giving rise to artifical ECMs (aECMs) with different morphological and biochemical characteristics that affect cell behaviour and ultimately tissue response. In this Chapter, the basic properties of fibrous proteins and their applications as coating material for biomaterials are described with special emphasis on collagen, including immobilization strategies for monomeric or fibrillar collagen species. Other fibrous proteins which do not naturally occur within the ECM (e.g. fibroin, keratin) are included because the presence of cell adhesion sequences has been reported for them. The final Section gives an outlook about the possible utilization of sophisticated aECMs.