Folding and self-assembly of short intrinsically disordered peptides and protein regions

Proteins and peptide fragments are highly relevant building blocks in self-assembly for nanostructures with plenty of applications. Intrinsically disordered proteins (IDPs) and protein regions (IDRs) are defined by the absence of a well-defined secondary structure, yet IDPs/IDRs show a significant biological activity. Experimental techniques and computational modelling procedures for the characterization of IDPs/IDRs are discussed. Directed self-assembly of IDPs/IDRs allows reaching a large variety of nanostructures. Hybrid materials based on the derivatives of IDPs/IDRs show a promising performance as alternative biocides and nanodrugs. Cell mimicking, in vivo compartmentalization, and bone regeneration are demonstrated for IDPs/IDRs in biotechnological applications. The exciting possibilities of IDPs/IDRs in nanotechnology with relevant biological applications are shown.

Automated summary

Proteins and peptide fragments play a crucial role in self-assembly for nanostructures, with intrinsically disordered proteins and protein regions showing significant biological activity. Experimental techniques and computational modeling procedures are used for characterization, leading to a wide variety of nanostructures and promising performance in biotechnological applications. Exciting possibilities for IDPs and IDRs in nanotechnology with relevant biological applications are demonstrated.