Peptide self-assembly can be used as a bottom-up approach to material fabrication. Although many different types of materials can be prepared from peptides, hydrogels are perhaps one of the most common. Gels typically result from the self-assembly of peptides into fibrillar networks. Controlling the structural morphology of these fibrils and the networks they form allows direct control over a given material's bulk properties. However, exerting this control is extremely difficult as the mechanistic rules that govern peptide self-assembly are far from being established. Conversely, several amyloidogenic proteins have been shown to self-assemble into fibrils using a mechanism known as domain swapping. Here, discrete units of secondary structure or even whole domains are exchanged (swapped) among discrete proteins during self-assembly to form extended networks with precise structural control. This review discusses several common mechanistic variations of domain swapping using naturally occurring proteins as examples. The possibility of using these principles to design peptides capable of controlled assembly and fibril formation leading to materials with targeted properties is explored.
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