Self-Assembling Peptides as Synthetic Extracellular Matrices

The self-assembling of biomolecules is a phenomenon commonly observed in biology, from DNA self-complementary double helix annealing, through protein aggregation or lipid membrane formation. Among them are included the proteins forming the extracellular matrix (ECM) of connective tissues, such as collagens, laminins, and fibronectins. Several self-assembling peptides have been molecular designed taking the assembling principles of Lysβ-21 and EAK16 as reference. The RAD16-I is used in this chapter to illustrate the self-assembling process. Currently, the use of self-assembling peptides has been implemented and verified to be an excellent scaffold for both in vitro and in vivo applications. The chapter first reviews several in vitro studies. Some of them involve the functional maintenance of hepatocytes in vitro, which is a major challenge since these cells rapidly lose their metabolic properties in culture.