An antiviral trap made of protein nanofibrils and iron oxyhydroxide nanoparticles

Palika, Archana; Armanious, Antonius; Rahimi, Akram; Medaglia, Chiara; Gasbarri, Matteo; Handschin, Stephan; Rossi, Antonella; Pohl, Marie O.; Busnadiego, Idoia; Gübeli, Christian; Anjanappa, Ravi B.; Bolisetty, Sreenath; Peydayesh, Mohammad; Stertz, Silke; Hale, Benjamin G.; Tapparel, Caroline; Stellacci, Francesco; Mezzenga, Raffaele

doi:10.1038/s41565-021-00920-5

Cited by 69 publications

(66 citation statements)

References 54 publications

(61 reference statements)

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“…An overall sustainability footprint was calculated by summing up the individual components as

100\% \cdot \sum\nolimits_{j = 1}^8 {{{( {\frac{i}{3}} )}_j} \cdot \frac{1}{8}}

, where each of the j = 8 discriminants carries a weight between 1/3 and 1 depending on the score i . [ 31 ] The overall sustainability footprint for meat, milk, and oat was around 46%, 63%, and 96%, respectively, demonstrating oat as the most sustainable source of protein among the considered cases.…”

Section: Resultsmentioning

confidence: 99%

“…To evaluate the ability of oat amyloid fibrils in removing gold and to compare them with β ‐lg ones, different membranes were prepared by using pure amyloid fibrils and in combination with activated carbon. [ 31b ] While the pure amyloid fibrils membranes were formed by vacuum filtration of 1 mL of 0.2 wt% fibril solutions on the surface of cellulose filters, the composite membranes were prepared by vacuum filtration of 1 mL of a homogenous aqueous mixture of 2 wt% amyloid fibril solution (1 mL) and 10 wt% activated carbon solution (2 mL). Then the as‐prepared membranes were used for gold removal from aqueous solutions by bench‐scale dead‐end vacuum filtration setup.…”

Section: Methodsmentioning

confidence: 99%

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Oat Plant Amyloids for Sustainable Functional Materials

Zhou

Peydayesh

et al. 2021

Advanced Science

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Amyloid functional materials from amyloid fibril building blocks, produced in vitro from amyloidogenic natural proteins or synthetic peptides, show diverse functionalities ranging from environmental science and biomedicine, to nanotechnology and biomaterials. However, sustainable and affordable sources of amyloidogenic proteins remain the bottleneck for large-scale applications, and to date, interest remains essentially limited to fundamental studies. Plant-derived proteins would be an ideal source due to their natural abundance and low environmental impact. Hereby oat globulin, the primary protein of oat plant (Avena sativa), is utilized to yield high-quality amyloid fibrils and functional materials based thereof. These fibrils show a rich multistranded ribbon-like polymorphism and a fibrillization process with both irreversible and reversible pathways. The authors furthermore fabricate oat-amyloid aerogels, films, and membranes for possible use in water purification, sensors, and patterned electrodes. The sustainability footprint of oat-amyloids against other protein sources is demonstrated, anticipating an environmentally-efficient platform for advanced materials and technologies.

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“…An overall sustainability footprint was calculated by summing up the individual components as

100\% \cdot \sum\nolimits_{j = 1}^8 {{{( {\frac{i}{3}} )}_j} \cdot \frac{1}{8}}

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Oat Plant Amyloids for Sustainable Functional Materials

Zhou

Peydayesh

et al. 2021

Advanced Science

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“…With respect to the non-structural viral proteins, well-defined targets are the 2C ATPase [95], the 2A pro [92], the 3C pro [99], and the 3D pol [103]. Virus binding can be specifically blocked with soluble receptor derivatives [149,150], and, more specifically, with highly charged multivalent nanoparticles [23,219], the polysaccharides iota-carrageenan [22,220], and PDS fibrils [25], either aggregating the virus or blocking its access to the cell. Additionally, virus uncoating can be prevented by the inhibition of membrane and cortical cytoskeleton rearrangements [148], activating the autophagy pathway [147], interfering with the maturation of endosomal vesicles [145], and, more specifically, for RVs only, by increasing the endosomal pH [221].…”

Section: Discussionmentioning

confidence: 99%

Rhinovirus Inhibitors: Including a New Target, the Viral RNA

Real-Hohn

Blaas

2021

Viruses

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Rhinoviruses (RVs) are the main cause of recurrent infections with rather mild symptoms characteristic of the common cold. Nevertheless, RVs give rise to enormous numbers of absences from work and school and may become life-threatening in particular settings. Vaccination is jeopardised by the large number of serotypes eliciting only poorly cross-neutralising antibodies. Conversely, antivirals developed over the years failed FDA approval because of a low efficacy and/or side effects. RV species A, B, and C are now included in the fifteen species of the genus Enteroviruses based upon the high similarity of their genome sequences. As a result of their comparably low pathogenicity, RVs have become a handy model for other, more dangerous members of this genus, e.g., poliovirus and enterovirus 71. We provide a short overview of viral proteins that are considered potential drug targets and their corresponding drug candidates. We briefly mention more recently identified cellular enzymes whose inhibition impacts on RVs and comment novel approaches to interfere with infection via aggregation, virus trapping, or preventing viral access to the cell receptor. Finally, we devote a large part of this article to adding the viral RNA genome to the list of potential drug targets by dwelling on its structure, folding, and the still debated way of its exit from the capsid. Finally, we discuss the recent finding that G‑quadruplex stabilising compounds impact on RNA egress possibly via obfuscating the unravelling of stable secondary structural elements.

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“…The technology used to produce whey protein nanofibrils-carbon hybrid membranes and granules has been deeply discussed in numerous earlier publications and will be no further discussed here. In short, hybrid membranes and granulated media were produced and kindly provided by BluAct Technologies GmbH, following earlier publication and patent protocols (17,18,(24)(25)(26). Fig.…”

Section: Methodsmentioning

confidence: 99%

“…Accordingly, it has become an emergency to identify a suitable, low energy consumption, highly efficient and safe technology that does not require large investments and can be used at the household level, specifically in close proximity of the mining areas. Protein nanofibrils generated from inexpensive milk proteins have shown unique binding properties to adsorb, via metal-ligand binding interactions, any type of heavy metal ions and metalloid, including arsenic, from polluted water in a non-selective, very general and unprecedented way [17][18][19][20][21][22][23][24]. This new technology is radically distinct from current technologies and shows all promises to bring a groundbreaking solution to this long-standing problem.…”

Section: Introductionmentioning

confidence: 99%