Crystallin Nanofibrils: A Functionalizable Nanoscaffold with Broad Applications Manufactured from Waste

Kaur, Manmeet; Roberts, S. J.; Healy, Jackie P.; Domigan, Laura; Vasudevamurthy, Madhusudan; Gerrard, Juliet A.; Sasso, Luigi

doi:10.1002/cplu.201500033

Cited by 7 publications

(10 citation statements)

References 87 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The self-assembly properties [ 1 , 4 , 5 ] and high stability [ 6 , 7 ] of amyloid fibrils suggest the potential to utilize them as bionanomaterials [ 8 ]. Previous research has demonstrated the functionalization of fibrils for various applications such as biosensors [ 9 , 10 , 11 , 12 , 13 ], nanowires [ 14 , 15 , 16 ], nanocomposites [ 17 , 18 ], thin films [ 19 ], nanoporous matrices [ 20 ], hydrogels [ 21 ], and aerogels [ 22 ]. Their stability over a broad-range of temperatures, pHs, solvents, and proteases, allows amyloid fibrils to be exploited for many applications [ 13 , 23 ].…”

Section: Introductionmentioning

confidence: 99%

“…This is a major constraint in translating laboratory scale conceptual applications to commercial products [ 19 , 20 , 21 , 24 , 25 ]. Low-cost, crude protein sources such as whey [ 25 ], soy [ 26 ], and crystallin proteins extracted from fish, bovine, and deer eye lenses, have been used for amyloid fibril formation and functionalization [ 12 , 27 , 28 ]. This study focuses on utilizing bovine blood as a low-cost protein source for amyloid fibril synthesis.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Amyloid Fibrils from Hemoglobin

et al. 2017

Self Cite

View full text Add to dashboard Cite

Amyloid fibrils are a class of insoluble protein nanofibers that are formed via the self-assembly of a wide range of peptides and proteins. They are increasingly exploited for a broad range of applications in bionanotechnology, such as biosensing and drug delivery, as nanowires, hydrogels, and thin films. Amyloid fibrils have been prepared from many proteins, but there has been no definitive characterization of amyloid fibrils from hemoglobin to date. Here, nanofiber formation was carried out under denaturing conditions using solutions of apo-hemoglobin extracted from bovine waste blood. A characteristic amyloid fibril morphology was confirmed by transmission electron microscopy (TEM) and atomic force microscopy (AFM), with mean fibril dimensions of approximately 5 nm diameter and up to several microns in length. The thioflavin T assay confirmed the presence of β-sheet structures in apo-hemoglobin fibrils, and X-ray fiber diffraction showed the characteristic amyloid cross-β quaternary structure. Apo-hemoglobin nanofibers demonstrated high stability over a range of temperatures (−20 to 80 °C) and pHs (2–10), and were stable in the presence of organic solvents and trypsin, confirming their potential as nanomaterials with versatile applications. This study conclusively demonstrates the formation of amyloid fibrils from hemoglobin for the first time, and also introduces a cost-effective method for amyloid fibril manufacture using meat industry by-products.

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Amyloid Fibrils from Hemoglobin

et al. 2017

Self Cite

View full text Add to dashboard Cite

show abstract

“…The aim of template directed amyloid fibril growth from surfaces is to increase the available surface area for enzyme immobilization, and to create an environment that is advantageous toward enzyme activity and stability. The use of other nanosupports such as nanoparticles, nanotubes, electrospun nanofibers, and nanoporous matrices have shown the ability to increase the available surface area for enzyme immobilization, while lowering mass transfer resistance . Template directed amyloid fibril growth allows the creation of self‐assembling nanomaterials, provides a means to collect amyloid fibrils, and if the surface assembled amyloid fibrils are functionalized with biomolecules, the biomolecules can be easily reused due to their surface attachment.…”

Section: Resultsmentioning

confidence: 99%

“…8 Many different supports exist for enzyme immobilization, and protein nanofibrils, such as amyloid fibrils, can act as a biomolecule nanoscaffold. [11][12][13][14][15][16] The intrinsic features of amyloid fibrils such as their nanometer size, chemical functionality arising from amino acid side chains and the ability to selfassemble, make amyloid fibrils an ideal candidate as a nanoscaffold. In this study, bovine insulin amyloid fibrils are used as a model amyloid fibril nanoscaffold.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of tobacco etch virus (TEV) protease on a high surface area protein nanofibril scaffold

Raynes

Domigan

Pearce

et al. 2018

Biotechnology Progress

Self Cite

View full text Add to dashboard Cite

Tobacco etch virus (TEV) protease is widely used for the removal of poly-histidine affinity tags from proteins. In solution, it is a one-time use enzyme for tag cleavage that has low stability, and is therefore a good candidate for immobilization. Amyloid fibrils can act as a versatile nanoscaffold by providing a large surface area for biomolecule immobilization. Immobilization of TEV protease to amyloid fibrils grown from the surface of a small glass bead, using physisorption, successfully immobilized active TEV protease. The bead retained activity over several uses and successfully cleaved a poly-histidine tag from several his-tagged proteins. This is first time that TEV protease has been immobilized to insulin amyloid fibrils, or any protein based support. Such functionalized surface assembled amyloid fibrils show promise as a novel nanosupport for the creation of functional bionanomaterials, for example, active surface coatings for the production of fine chemicals, chemical detoxification, or biosensing. Insulin amyloid fibrils provide a new nanosupport for the immobilization of TEV protease, which could allow for the reuse of the enzyme, saving on production costs for recombinantly expressed poly-histidine tagged proteins. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 2018.

show abstract

“…As a final comment, although outside the scope of this review, amyloid nanofibril functionalization with diverse chemical groups or biomolecules is to be mentioned for its high potential to provide novel functional bionanomaterials, as reviewed elsewhere [163,172]. For instance, semi-conductive peptide nanofibrils [173] or enzyme immobilization on protein nanofibrils have been successfully obtained via specific chemical functionalization steps [174]. Diverse applications may emerge from this research, from novel nanomaterials for nanoelectronics to biosensing in medical sciences.…”

Section: Conclusion: Towards Amyloid Disease Therapy and Bionanomatermentioning

confidence: 99%

Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design

et al. 2017

View full text Add to dashboard Cite

Amyloid nanofibrils are ubiquitous biological protein fibrous aggregates, with a wide range of either toxic or beneficial activities that are relevant to human disease and normal biology. Protein amyloid fibrillization occurs via nucleated polymerization, through non-covalent interactions. As such, protein nanofibril formation is based on a complex interplay between kinetic and thermodynamic factors. The process entails metastable oligomeric species and a highly thermodynamically favoured end state. The kinetics, and the reaction pathway itself, can be influenced by third party moieties, either molecules or surfaces. Specifically, in the biological context, different classes of biomolecules are known to act as catalysts, inhibitors or modifiers of the generic protein fibrillization process. The biological aggregation modifiers reviewed here include lipid membranes of varying composition, glycosaminoglycans and metal ions, with a final word on xenobiotic compounds. The corresponding molecular interactions are critically analysed and placed in the context of the mechanisms of cytotoxicity of the amyloids involved in diverse pathologies and the non-toxicity of functional amyloids (at least towards their biological host). Finally, the utilization of this knowledge towards the design of bio-inspired and biocompatible nanomaterials is explored.

show abstract

Crystallin Nanofibrils: A Functionalizable Nanoscaffold with Broad Applications Manufactured from Waste

Cited by 7 publications

References 87 publications

Amyloid Fibrils from Hemoglobin

Amyloid Fibrils from Hemoglobin

Immobilization of tobacco etch virus (TEV) protease on a high surface area protein nanofibril scaffold

Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design

Contact Info

Product

Resources

About