Amyloid‐Like Fibrils: Origin, Structure, Properties, and Potential Technological Applications

Taboada, Pablo; Barbosa, Sílvia; Juárez, Josué; Alatorre-Meda, Manuel; Mosquera, Víctor X.

doi:10.1002/9781118523063.ch12

Cited by 4 publications

(3 citation statements)

References 503 publications

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“…This behaviour is described for other non-ionic anionic surfactants and polymers, and for amylogenic oligomers. 34,35,21 Oligomers shape's transition occurs with increasing oligomers size.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages

Herrera

Pizzuto

Lonez

et al. 2018

Nanomedicine: Nanotechnology, Biology and Medicine

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Gliadin, an immunogenic protein present in wheat, is not fully degraded by humans and after the normal gastric and pancreatic digestion, the immunodominant 33-mer gliadin peptide remains unprocessed. The 33-mer gliadin peptide is found in human faeces and urine, proving not only its proteolytic resistance in vivo but more importantly its transport through the entire human body. Here, we demonstrate that 33-mer supramolecular structures larger than 220 nm induce the overexpression of nuclear factor kappa B (NF-κB) via a specific Toll-like Receptor (TLR) 2 and (TLR) 4 dependent pathway and the secretion of pro-inflammatory cytokines such as IP-10/CXCL10 and TNF-α. Using helium ion microscopy, we elucidated the initial stages of oligomerisation of 33-mer gliadin peptide, showing that rod-like oligomers are nucleation sites for protofilament formation. The relevance of the 33-mer supramolecular structures in the early stages of the disease is paving new perspectives in the understanding of gluten-related disorders.

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Section: Accepted Manuscriptmentioning

confidence: 99%

Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages

Herrera

Pizzuto

Lonez

et al. 2018

Nanomedicine: Nanotechnology, Biology and Medicine

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“…Such protrusions, referred to as filopodia or pseudopods (50–500 nm in diameter), sense the surface in contact with the cell for the presence of adhesive proteins where to attach by virtue of integrins (integrins are often found in the tips or along the shafts of filopodia). − Cell adherence and movement then occurs in the direction of the emerging contact points through retraction of the attached pseudopods . Based on this explanation, we hypothesize that CVD membranes provide focal locations for filopodial attachment by presenting nanometric features orthogonal to the membrane surface along which proteins recognized by integrins are deposited (i.e., the characteristic heights of the ridges depicted in Figure ). , As shown in previous publications, this scenario can fairly be anticipated given the fact that proteins readily accumulate by the curvature of nanofeatured ridges like ours and other similar bodies with comparable dimensions; , being this curvature precisely the place where filopodia preferentially accommodate . On the contrary and absent of such noticeable protuberances, nontreated (CH) and solution cross-linked membranes (CH02GEN-S) appear not to offer cells with the required retention points for proteins and pseudopods, hampering in consequence the cell adherence and proliferation.…”

Section: Results and Discussionmentioning

confidence: 99%

Enhanced Cell Affinity of Chitosan Membranes Mediated by Superficial Cross-Linking: A Straightforward Method Attainable by Standard Laboratory Procedures

Rodríguez-Velázquez¹,

Silva²,

Taboada³

et al. 2013

Biomacromolecules

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It is well accepted that the surface modification of biomaterials can improve their biocompatibility. In this context, techniques like ion etching, plasma-mediated chemical functionalization, electrospinning, and contact microprinting have successfully been employed to promote the cell adhesion and proliferation of chitosan (CH) substrates. However, they prove to be time-consuming, highly dependent on environmental conditions, and/or limited to the use of expensive materials and sophisticated instruments not accessible to standard laboratories, hindering to a high extent their straightforward application. Filling this gap, this paper proposes the superficial cross-linking of CH as a much simpler and accessible means to modify its superficial properties in order to enhance its cellular affinity. CH membranes were prepared by solvent casting followed by a cross-linking step mediated by the chemical vapor deposition (CVD) of glutaraldehyde (GA). The membranes were characterized against non- and solution cross-linked membranes in terms of their mechanical/surface properties and biological performance. Among others, the CVD membranes proved (i) to be more mechanically stable against cell culture and sterilization than membranes cross-linked in solution and (ii) to prompt the adherence and sustained proliferation of healthy cells to levels even superior to commercial tissue culture plates (TCPs). Accordingly, the CVD cross-linking approach was demonstrated to be a simple and cost-effective alternative to the aforementioned conventional methods. Interestingly, this concept can also be applied to other biomaterials as long as GA (or other volatile components alike) can be employed as a cross-linker, making possible the cross-linking reaction at mild experimental conditions, neither requiring sophisticated lab implements nor using any potentially harmful procedure.

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“…10 Structurally, amyloid fibrils are composed of b-sheets formed by the structural transition of the helical structure and are categorized as supramolecular polymers of b-strands stacked perpendicularly to the fibrils on their long axis. 11 Amyloids are insoluble accumulations of fibrils formed by various independent proteins such as Ab1-40, a-syn, insulin and peptides. 12,13 Apart from pathologically associated proteins such as amyloid b (Ab1-40), tau and a-synuclein (a-syn), several other proteins also form amyloid fibrils at high concentrations and under destabilizing conditions.…”

Section: Introductionmentioning

confidence: 99%

Advancements in amyloid-based biological materials for healthcare, environmental and sensing applications

Yadav,

Padhy,

Singh

et al. 2024

Mater. Adv.

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Amyloid‐Like Fibrils: Origin, Structure, Properties, and Potential Technological Applications

Cited by 4 publications

References 503 publications

Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages

Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages

Enhanced Cell Affinity of Chitosan Membranes Mediated by Superficial Cross-Linking: A Straightforward Method Attainable by Standard Laboratory Procedures

Advancements in amyloid-based biological materials for healthcare, environmental and sensing applications

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