Figure 1: Genetic programming and modularity of the BIND system.
From: Programmable biofilm-based materials from engineered curli nanofibres
In the BIND platform, ΔcsgA cells heterologously express and secrete fusion proteins consisting of an amyloidogenic domain (CsgA, shown in orange) and a functional peptide domain (green). This secreted fusion protein self-assembles into an extracellular network of amyloid nanofibres that are anchored onto the cell surface, resulting in a biofilm material with programmed non-natural functions. A three-dimensional protein model is shown of the self-assembling and functional peptide domains, using homology model protein threading of the CsgA sequence onto an AgfA structure. An example peptide domain, SpyTag (see Table 1), is shown in green and the six-residue flexible linker in grey. The peptide structure was predicted using PepFold and all structural manipulation performed in PyMol.
