In biotechnology, generating functional synthetic amyloid structures to form nanostructures by imitating the natural generation process is not new. The assembly of proteins into stable fibres allows creating supramolecular shapes that no isolated protein can create, and which are used as nanoconductors, photovoltaic structures, biosensors and catalysts.

Quite recently, researchers began synthesizing prion protein sequences to form nanomaterials. The interest in these sequences lies in the fact that the proteins assemble in a slower and more controlled manner, forming highly ordered, nontoxic nanostructures. However, the fact that the sequence is so long, with over 150 amino acids, makes it very difficult and expensive to synthesise.

“We have demonstrated that an adequate design can permit the size of synthetic prion sequences to be reduced down to only 7 amino acids, while conserving the same properties. The four peptides we have fabricated are the shortest structures of this type created until now, and are capable of forming stable fibril assemblies,” says Salvador Ventura, researcher at the IBB and the UAB Department of Biochemistry and Molecular Biology.