Two-dimensional sheets composed of collagen-mimetic peptides on the nanoscale that are highly-ordered and self-assembling.
- Thermal stability, sheet thickness, and sheet dimensions can be controlled through the peptide sequence and preparative conditions.
Collagens are used in a number of consumer and biomedical products including cosmetics, tissue repair, wound management, burn treatment, drug delivery, sutures, tissue engineering, and vasculature and valve replacements. Currently, collagen derivatives for medical applications originate primarily from animal sources; however, the development of synthetic collagen-mimetic materials could be designed and tailored for specific biomedical applications and functions. In particular, these mimetics could exploit higher-order structures and assembly mechanisms that do not occur in natural collagens.
Collagen is the most abundant protein in vertebrate systems and occupies a biologically critical functional role as the main structural component of the extracellular matrix. As such, it is responsible for tissue development and the maintenance of tissue structural integrity. Emory researchers have developed a method to generate highly-ordered two-dimensional peptide sheets. Most collagen-mimetic peptides lack a structural mechanism to ensure correct alignment of chains upon self-association that is inherently encoded within the protein sequences of native collagens. The peptide nanosheets can self-assemble into structurally defined two-dimensional nano-scale to micro-scale assemblies. The thermal stability, sheet thickness, and sheet dimensions can be controlled through the peptide sequence and the preparative conditions. Finally, the peptides can be functionalized at either the N-terminus or C-terminus to functionalize the surface of the nano-scale sheets.
Collagen-mimetic nanosheets and associated methods have been described.
Publication: Yu et al. 2011. Soft Matter. 7:7927-7938.