Amyloid self‐assembling peptides: Potential applications in nanovaccine engineering and biosensing

Abstract

AbstractLiving organisms are an inestimable source of inspiration for the design of biomaterials and nanostructures for medical and technological applications. Amyloids, which were historically associated with diseases, have recently been recognized as a biological structure that performs vital physiological functions in host organisms, highlighting their potential as life‐inspired assemblies. Amyloids are highly organized proteinaceous assemblies characterized by a cross‐β‐sheet quaternary conformation. The mechanical, physical, and biological properties of amyloids suggest that these nanostructures hold great potential as soft materials, nanoparticles, and biomatrices. This potential is associated with many characteristics, including the spontaneous self‐assembly of many polypeptide sequences, high mechanical resistance, biocompatibility, biodegradability as well as thermal, chemical, and enzymatic stability. Moreover, peptide‐based amyloid assemblies can efficiently be obtained by standard solid phase peptide synthesis and orthogonally functionalized with a wide range of biomolecules, such as large proteins and DNA. In this review, after briefly introducing the amyloid structure and the mechanisms of self‐assembly, we describe approaches to identify and design short self‐assembling amyloidogenic peptides. Afterward, we introduce strategies used to functionalize amyloid materials and we highlight some relevant examples in the development of nanovaccines and biosensors.