Minimalist biostructures designed to create nanomaterials

Researchers from the IBB-UAB and from the ICMAB-CSIC have obtained four molecules of only seven amino acids with the ability to self-assemble, which enables a fast and non expensive process to obtain nanomaterials for biomedical and nanotechnological purposes. They have used them to create one of the most resistant bionanomaterials described until now.

 

The four peptides formed by seven amino acids, an pictures (right) of the nanomaterials obtained with them Researchers of the Institute of Biotechnology and Biomedicine (IBB-UAB) have generated 4 peptides -molecules smaller than proteins - capable of self-assembling in a controlled way to form nanomaterials. The research, published in the journal ACS Nano, was conducted by Salvador Ventura, Marta Díaz Caballero and Susanna Navarro (IBB-UAB), and included the collaboration of Isabel Fuentes and Francesc Teixidor (Institute of Materials Science of Barcelona, ICMAB-CSIC).

The new molecules are formed by a chain of seven amino acids, each of which are made up of only two different amino acids; thus, significantly speeding up and reducing the price of the process of creation of functional synthetic amyloid structures with which to generate nanomaterials to be used in biomedicine and nanotechnology.

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 which no isolated protein can create, and which are used as nanoconductors, photovoltaic structures, biosensors and catalysts.

Quite recently, prion protein sequences – also amyloids – began to be imitated 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 non-toxic nanostructures. However, the fact that the sequence is so long, with over 150 amino acids, makes it very difficult and expensive to synthesise.

The scientists have demonstrated in this study that an adequate design can permit the size of synthetic prion sequences to be reduced down to only seven amino acids, while conserving the same properties. The four peptides they have fabricated are the shortest structures of this type created until now and capable of forming stable fibril assemblies.