Patterned Amyloid Materials Integrating Robustness and Genetically Programmable Functionality

Abstract

The precise manipulation, localization, and assembly of biological and bioinspired molecules into organized structures have greatly promoted material science and bionanotechnology. Further technological innovation calls for new patternable soft materials with the long-sought qualities of environmental tolerance and functional flexibility. Here, we report a patterned amyloid material (PAM) platform for producing hierarchically ordered structures that integrate these material attributes. This platform, combining soft lithography with generic amyloid monomer inks (consisting of genetically engineered biofilm proteins dissolved in hexafluoroisopropanol), along with methanol-assisted curing, enables the spatially controlled deposition and in situ reassembly of amyloid monomers. The resulting patterned structures exhibit spectacular chemical and thermal stability and mechanical robustness under harsh conditions. The PAMs can be programmed for a vast array of multilevel functionalities, including anchoring nanoparticles, enabling diverse fluorescent protein arrays, and serving as self-supporting porous sheets for cellular growth. This PAM platform will not only drive innovation in biomanufacturing but also broaden the applications of patterned soft architectures in optics, electronics, biocatalysis, analytical regents, cell engineering, medicine, and other areas.

Patterning of protein‐based materials

“…For instance, a functional amyloid protein CsgA was used to develop a material platform for producing hierarchically ordered fibrous mictrostructures. [ 44 ] CsgA is a protein expressed in Escherichia coli , which naturally self‐assembles into functional amyloid fibers forming an extracellular matrix encapsulating the bacteria within a biofilm. [ 45 ] Using a combination of soft lithography with CsgA monomer inks, the protein could be transferred onto surfaces.…”

“…The robustness of the CsgA self‐assembly enabled also the fusion with tags such as a polyhistidine‐tag fused to the C‐terminus of CsgA for binding of inorganic nanoparticles, or CsgA‐CBD with a fused chitin‐binding domain (CBD) acting as a linker between chitin and CsgA nanofibers and enabling self‐supporting patterned porous sheets. [ 44 ]…”

Nanoscale Surface Topography Modulates hIAPP Aggregation Pathways at Solid–Liquid Interfaces

“…While it was already shown thirty years ago that the presence of interfaces can also stimulate protein and peptide aggregation [ 31 ], surface- and interface-related effects have only recently become a focus of attention [ 32 , 33 , 34 ]. This recent development was mostly motivated by the potential of nanoparticle-based strategies to mitigate amyloid-associated diseases [ 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 ], as well as by promising applications of amyloid fibrils in materials’ synthesis [ 44 , 45 , 46 , 47 , 48 ]. Nevertheless, the manifold effects of the physicochemical surface properties on amyloid aggregation and the involved molecular mechanisms are far from understood [ 33 , 34 ].…”

Amyloid hybrid membranes for bacterial & genetic material removal from water and their anti-biofouling properties

“…29 Therefore, their removal from drinking water is absolutely necessary, but due to their dimensions smaller than 1 nm, it is difficult to remove them in current water treatment processes, even via ultraltration, microltration and nanoltration. 30 Earlier studies revealed that amyloid hybrid membranes (AHM) may be able to remove bacteria by a size-exclusion mechanism, [31][32][33][34] but we did not investigate this effect systematically, nor considered whether genetic material from biological contamination could be removed from water by the same membranes. This paper focuses on the removal efficiency of the amyloid hybrid membranes for both bacteria and genetic material by the systematic investigation.…”