Silk-based peptide

Another, promising avenue to understand silk protein conformation and assembly is the use of model peptides. Although not recent (Fraser and MacRae, 1973 Lotz et al., 1974), studies of silk-based peptide from chemical synthesis, DNA recombinant technology, and computer simulation (Anderson et al., 1994 Asakura et al., 2003 Fahnestock et al., 2000 Fossey et al., 1991 Heslot, 1998 Kaplan, 1998 Wilson et al., 2000) have shown that selected repeats of silk proteins can be transformable hydrogels, elastomers, or regular thermoplastics and that with a proper design they can function as diverse molecular machines (Altman et al., 2003 Heslot, 1998 Kaplan, 1998 Urry, 1998). 

Sheets also play an important role in the construction of peptide-based functional nanohbrous materials. /3-sheets are preferred over a-helices as molecular building blocks in the fabrication of artificial nanostructured materials perhaps because of the growing interest in understanding the self-assembly of two types of namral /3-sheet products silk protein and amyloid-Uke /3-sheets. Furthermore, extended /3-sheet conformation is relatively easy to achieve. Indeed, preventing their formation, particularly in high concentration or at high temperature, can be difficult in both synthetic and natural constructs. 

Paul van der Schoot, Nucleation and Co-Operativity in Supramolecular Polymers Michael J. McPherson, Kier James, Stuart Kyle, Stephen Parsons, and Jessica Riley, Recombinant Production of Self-Assembling Peptides Boxun Leng, Lei Huang, and Zhengzhong Shao, Inspiration from Natural Silks and Their Proteins Sally L. Gras, Surface- and Solution-Based Assembly of Amyloid Fibrils for Biomedical and Nanotechnology Applications... 

Peptide-based stmctural materials have often been designed by using consensus peptide sequences derived from naturally occurring structural proteins such as collagen, elastin, and silk as building blocks. Most of these building... 

Chen, K., Shi, P., Teh, T.K., Toh, S.L., Gob, J.C., 2013. In vitro generation of a multilayered osteochondral construct with an osteochondral interface using rabbit bone marrow stromal cells and a silk peptide-based scaffold. J. Tissue Eng. Regen. Med. 10 (4), 284—293. 

Chimeric (fusion) proteins that incorporate the R5 peptide have been synthesized to control and precipitate silica nanoparticles. Po Foo and coworkers have utilized a two-component chimeric protein consisting of the R5 polypeptide (from C. fusiformis) and the self-assembling domain based on the consensus repeat in the major ampullate spidroin protein 1 (MaSpl) of Nephila clavipes spider dragline silk [64]. MaSpl forms highly stable P-sheet secondary stmctures that can be spun into intricate fibers which, when fused with the sihca-templating R5-peptide, allow for the formation of film-like and fibrous silica structures (Figure 1.18). 

---