Abstract
Protein amyloid nanofibers provide a biocompatible platform for the development of functional nanomaterials. However, the functionalities generated up to date are still limited. Typical building blocks correspond to aggregation-prone proteins and peptides, which must be modified by complex and expensive reactions post-assembly. There is high interest in researching alternative strategies to tailor amyloid-based nanostructures’ functionality on demand. In the present study, the biotin-streptavidin system was exploited for this purpose. Prion-inspired heptapeptides (Ac-NYNYNYN-NH2, Ac-QYQYQYQ-NH2, and Ac-SYSYSYS-NH2) were doped with biotin-conjugated counterparts and assembled into amyloid-like fibers under mild conditions. The scaffolds’ versatile functionalization was demonstrated by decorating them with different streptavidin conjugates, including gold nanoparticles, quantum dots, and enzymes. In particular, they were functionalized with peroxidase or phosphatase activities using streptavidin conjugated with horseradish peroxidase and alkaline phosphatase, respectively. Modification of amyloid-like nanostructures has generally been restricted to the addition of a single protein moiety. We functionalized the fibrils simultaneously with glucose oxidase and horseradish peroxidase, coupling these activities to build up a nanostructured glucose biosensor. Overall, we present a simple, modular, and multivalent approach for developing amyloid-based nanomaterials functionalized with any desired combination of chemical and biological moieties.
Highlights
Molecular self-assembly is a leading bottom-up strategy for fabricating novel complex nanostructures.[1−3] This approach exploits the selective recognition between molecular building units to fabricate novel architectures with nanometric dimensions
In the design of an amyloid-based biotin-streptavidin system, it was important to avoid steric impairments that might interfere with the self-assembly or reduce the accessibility of streptavidin-conjugated partners to biotinylated peptides once they become embedded into the amyloid fibers
The incorporation of the biotin moieties to the nanofibers occurs during assembly and does not require the post-assembly modification of fibrillar matrices reported in previous studies.[43−45] due to their reduced size, both nonbiotinylated and biotinylated peptides can be commercially acquired with high purity at low cost
Summary
Molecular self-assembly is a leading bottom-up strategy for fabricating novel complex nanostructures.[1−3] This approach exploits the selective recognition between molecular building units to fabricate novel architectures with nanometric dimensions Bionanomaterials, such as protein nanofibers, offer significant advantages over inorganic assemblies since they provide a cost-effective and environmentally friendly way to produce versatile biocompatible nanomaterials.[4,5] Among them, amyloid fibrils have been gathering considerable attention as biocompatible functional materials[3,6−9] and for their application as scaffolds in tissue engineering.[10,11] They are held by densely packed, hydrogen-bonded β-sheets,[12] and this distinctive supramolecular configuration endows them with a rigid internal order that results in nanostructures with high strength, stability, and high-morphological aspect ratios,[13] which, together with their insolubility in aqueous media, make them optimal materials for bionanotechnological applications.[3,14]. In contrast to inorganic nanoparticles or carbon nanotubes, these prioninspired biocompatible nanostructures are formed under mild
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