Structural and functional diversity among amyloid proteins: Agents of disease, building blocks of biology, and implications for molecular engineering

Abstract

Amyloids have long been associated with protein dysfunction and neurodegenerative diseases, but recent research has demonstrated that some organisms utilize the unique properties of the amyloid fold to create functional structures with important roles in biological processes. Additionally, new engineering approaches have taken advantage of amyloid structures for implementation in a wide variety of materials and devices. In this review, the role of amyloid in human disease is discussed and compared to the functional amyloids, which serve a largely structural purpose. We then consider the use of amyloid constructs in engineering applications, including their utility as building blocks for synthetic biology and molecular engineering. Biotechnol. Bioeng. 2017;114: 7-20. © 2016 Wiley Periodicals, Inc.

Protein Engineering Reveals Mechanisms of Functional Amyloid Formation in Pseudomonas aeruginosa Biofilms

“…1a). Insoluble amyloid deposits form as a result of protein folding dysfunction in diseases like Alzheimer’s and Parkinson’s, but recent evidence suggests that several microbes intentionally produce amyloid fibrils to serve functional roles [10]. Biofilm-associated bacteria, in particular, utilize amyloids as a building material to reinforce the EM and resist dispersion by chemical or mechanical agents [8, 11].…”

Self‐assembly of two hydrophobins from marine fungi affected by interaction with surfaces

“…These assemblies differently graft surfaces with opposite wettability with different resistance to harsh washing. The knowledge of self‐assembly mechanism and boundary condition requirements for amyloid aggregation on the surfaces, (Accardo et al, ; Bellucci et al, , ; Du et al, ; Lin et al, ; Moores et al, ; Shaw et al, ; Vácha et al, ; Zhou et al, ) open the way to molecular level design of protein‐based devices for industrial and biomedical applications (Bleem and Daggett, ).…”

“…These assemblies differently graft surfaces with opposite wettability with different resistance to harsh washing. The knowledge of self-assembly mechanism and boundary condition requirements for amyloid aggregation on the surfaces, (Accardo et al, 2015;Bellucci et al, 2016Bellucci et al, , 2017Du et al, 2015;Lin et al, 2014;Moores et al, 2011;Shaw et al, 2012;V acha et al, 2014;Zhou et al, 2013) open the way to molecular level design of protein-based devices for industrial and biomedical applications (Bleem and Daggett, 2017). This work was supported by a grant from the Ministero dell'Universit a e della Ricerca Scientifica-Industrial research project "Development of green technologies for the production of BIO-chemicals and their use in the preparation and industrial application of POLImeric materials from agricultural biomasses cultivated in a sustainable way in Campania (BioPoliS)" PON03PE 00107 1, funded within the framework of Operative National Program Research and Competitiveness 2007D.…”

“…Proteins can form amyloid aggregates which are exceptionally stable to chemical depolymerization and to mechanical deformation (Choi et al, 2015;Knowles and Buehler, 2011;Lara et al, 2012;Usov and Mezzenga, 2014). These structures, thanks to their unique properties and their nanoscale size, are suitable building blocks of advanced bio-nanomaterials (Amit et al, 2012;Bleem and Daggett, 2017;Cherny and Gazit, 2008;Knowles and Mezzenga, 2016;Kumar et al, 2014;Reynolds et al, 2014). They find applications in nanodevices, biosensors, (Hauser et al, 2014;Piscitelli et al, 2017a) nanocomposites, (Li et al, 2012(Li et al, , 2014 drug delivery, (Bolisetty et al, 2014;Seras-Franzoso et al, 2016;Unzueta et al, 2017), and catalysis Piscitelli et al, 2017b).…”

“…The growth of amyloid fibrils and their stacking into plaques in human tissues is often associated with neurodegenerative disorders such as Alzheimer's and Parkinson's disease (Chiti and Dobson, 2006;Eisenberg and Jucker, 2012). However, the discovery in nature of functional amyloid fibrils in several organisms, including humans, endowed with important biological functions rather than associated with degenerative processes, has attracted the attention of many researchers intrigued by the features of these high-performance and environmentally benign structures (Bleem and Daggett, 2017;Fowler et al, 2007;Knowles and Buehler, 2011;Knowles and Mezzenga, 2016). Some proteins produced by fungi, the hydrophobins, belong to the family of functional amyloids (Bleem and Daggett, 2017;Gebbink et al, 2005;Macindoe et al, 2012).…”