David Kaplan1
Tufts University1
Silk proteins are unique polymer systems with polymorphic behavior. This is driven by the peptide repeats and their amphiphilicity and organization, resulting in self-assembly in aqueous, ambient conditions into regular secondary and higher order structures. In nature, this process leads to mechanically robust fibers, while in the laboratory new material outcomes are achieved to optimize structure-function, thus, expanding on the template initially provided from nature. Experimental paths include modulating native processing conditions related to assembly, incorporating enzymatic crosslinking, exploiting bioengineering strategies, and the inclusion of second polymers or additives. Control of nanostructures in silks is key to these new functional silk materials, where modeling and experiment coexist to achieve silk nanoarchitectures and new material systems.