Amyloid-based nanosensors and nanodevices

Hauser, Charlotte; Maurer‐Stroh, Sebastian; Martins, Ivo C.

doi:10.1039/c4cs00082j

Cited by 161 publications

(191 citation statements)

References 195 publications

(338 reference statements)

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“…However, the challenges include (i) identifying protein segments with high potential for forming amyloid fibers, (ii) controlling the amyloid formation, and (iii) fine-tuning the design at the molecular level to achieve an accurate performance for the application of interest. 9,11,31 Here we propose a general method for the design of functional amyloid, based on the growing structure database of amyloid-forming peptides. Structure-based design has been an efficient method for finding molecules that interfere with protein activities and interactions.…”

Section: ■ Introductionmentioning

confidence: 99%

Structure-Based Design of Functional Amyloid Materials

et al. 2014

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Amyloid fibers, once exclusively associated with disease, are acquiring utility as a class of biological nanomaterials.Here we introduce a method that utilizes the atomic structures of amyloid peptides, to design materials with versatile applications. As a model application, we designed amyloid fibers capable of capturing carbon dioxide from flue gas, to address the global problem of excess anthropogenic carbon dioxide. By measuring dynamic separation of carbon dioxide from nitrogen, we show that fibers with designed amino acid sequences double the carbon dioxide binding capacity of the previously reported fiber formed by VQIVYK from Tau protein. In a second application, we designed fibers that facilitate retroviral gene transfer. By measuring lentiviral transduction, we show that designed fibers exceed the efficiency of polybrene, a commonly used enhancer of transduction. The same procedures can be adapted to the design of countless other amyloid materials with a variety of properties and uses.

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Section: ■ Introductionmentioning

confidence: 99%

Structure-Based Design of Functional Amyloid Materials

et al. 2014

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“…Several applications are being considered for using amyloids as nanowires and nanotubes for electronics, as nanosensors, as amyloid-based gels in cell adhesion and wound healing, and as drug delivery systems (96).…”

Section: Biotechnological Applications Of Biofilm Amyloid Fibersmentioning

confidence: 99%

Amyloid Structures as Biofilm Matrix Scaffolds

2016

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bRecent insights into bacterial biofilm matrix structures have induced a paradigm shift toward the recognition of amyloid fibers as common building block structures that confer stability to the exopolysaccharide matrix. Here we describe the functional amyloid systems related to biofilm matrix formation in both Gram-negative and Gram-positive bacteria and recent knowledge regarding the interaction of amyloids with other biofilm matrix components such as extracellular DNA (eDNA) and the host immune system. In addition, we summarize the efforts to identify compounds that target amyloid fibers for therapeutic purposes and recent developments that take advantage of the amyloid structure to engineer amyloid fibers of bacterial biofilm matrices for biotechnological applications.

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“…Their highly repetitive and ordered architecture, in particular for the short peptide fibrils, exhibits favorable properties including high thermal stability and stiffness, biocompatibility, controllable self-assembly, surface patterning and integration of functionality, and inexpensive production by chemical synthesis (11)(12)(13). These exceptional properties promote the exploitation of amyloid fibril as an emerging class of bionanomaterials (14).…”

mentioning

confidence: 99%

Tunable assembly of amyloid-forming peptides into nanosheets as a retrovirus carrier

Dai

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

130

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Using and engineering amyloid as nanomaterials are blossoming trends in bionanotechnology. Here, we show our discovery of an amyloid structure, termed "amyloid-like nanosheet," formed by a key amyloid-forming segment of Alzheimer's Aβ. Combining multiple biophysical and computational approaches, we proposed a structural model for the nanosheet that is formed by stacking the amyloid fibril spines perpendicular to the fibril axis. We further used the nanosheet for laboratorial retroviral transduction enhancement and directly visualized the presence of virus on the nanosheet surface by electron microscopy. Furthermore, based on our structural model, we designed nanosheet-forming peptides with different functionalities, elucidating the potential of rational design for amyloid-based materials with novel architecture and function.functional amyloid material | peptide self-assembly | nanosheet | retrovirus transduction | beta-amyloid N umerous proteins and polypeptides have been found to selfassemble into amyloid fibrils under certain conditions (1). They are associated not only with dozens of devastating diseases including Alzheimer's and Parkinson's diseases (2) but are integral to many biological processes such as hormone storage, signal transduction, and cell surface adhesion (3-5). Separate from the context of their parent proteins, synthesized peptide segments can self-assemble into amyloid-like fibrils in vitro as well (6, 7). Fibrils formed by diverse proteins and peptides all share a common cross-β structure, composed of interdigitated β-sheets termed "the zipper-like fibril spine" (8, 9). The self-assembly process is a consequence of backbone hydrogen bonding for the single β-sheet layer formation and side-chain interaction (e.g., hydrophobic interaction, π-stacking, and van der Waals) for pairing β-sheet layers together (10). Their highly repetitive and ordered architecture, in particular for the short peptide fibrils, exhibits favorable properties including high thermal stability and stiffness, biocompatibility, controllable self-assembly, surface patterning and integration of functionality, and inexpensive production by chemical synthesis (11-13). These exceptional properties promote the exploitation of amyloid fibril as an emerging class of bionanomaterials (14).Several studies have demonstrated that natural amyloidogenic and designed amphiphilic peptides are capable of self-assembling into nanostructures with topographies including fibril, film, nanotube, hydrogel, and liquid crystals (15-21), and these nanostructures have been used for nanowires, biosensors, 3D culturing, environmental carbon capture, retroviral gene transfer, light harvesting, and catalysis (22-26). Amyloid fibrils were also hybridized with other nanomaterials such as graphene and DNA origami in hopes of creating new properties and functions (27)(28)(29). In this study, we expand the amyloid material field's scope by the finding, structure characterization, and functionalization of a previously unidentified architecture-the amyloid-lik...

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Amyloid-based nanosensors and nanodevices

Cited by 161 publications

References 195 publications

Structure-Based Design of Functional Amyloid Materials

Structure-Based Design of Functional Amyloid Materials

Amyloid Structures as Biofilm Matrix Scaffolds

Tunable assembly of amyloid-forming peptides into nanosheets as a retrovirus carrier

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