Fabrication of amyloid peptide micro‐arrays using laser‐induced forward transfer and avidin‐biotin mediated assembly

Dinca, Valentina; Kasotakis, Emmanouil; Mourka, Areti; Ranella, Anthi; Farsari, Maria; Mitraki, Anna; Fotakis, C.

doi:10.1002/pssc.200780187

Cited by 8 publications

(6 citation statements)

References 24 publications

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“…This was further confirmed experimentally, since peptides having cysteine substituted at these positions (the same ones used in this work) can self-assemble into fibrils that template metal nanoparticle formation in solution . These fibrils can also attach to surfaces functionalized with free-thiol modifying reagents, such as iodoacetamide. , We therefore assume that the cysteine-containing fibrils attach to the gold surface through sulfur−gold interactions; however they still carry at their solution-exposed side cysteine groups available for interaction with copper ions. Based on these results, NC nanofibrils and gold electrodes were selected for the further development of the biosensor.…”

Section: Resultssupporting

confidence: 64%

“…30 These fibrils can also attach to surfaces functionalized with free-thiol modifying reagents, such as iodoacetamide. 34,35 We therefore assume that the cysteine-containing fibrils attach to the gold surface through sulfurÀgold interactions; however they still carry at their solution-exposed side cysteine groups available for interaction with copper ions. Based on these results, NC nanofibrils and gold electrodes were selected for the further development of the biosensor.…”

Section: ' Materials and Methodsmentioning

confidence: 99%

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Development of an Electrochemical Metal-Ion Biosensor Using Self-Assembled Peptide Nanofibrils

Viguier

Zór

Kasotakis

et al. 2011

ACS Appl. Mater. Interfaces

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This article describes the combination of self-assembled peptide nanofibrils with metal electrodes for the development of an electrochemical metal-ion biosensor. The biological nanofibrils were immobilized on gold electrodes and used as biorecognition elements for the complexation with copper ions. These nanofibrils were obtained under aqueous conditions, at room temperature and outside the clean room. The functionalized gold electrode was evaluated by cyclic voltammetry, impedance spectroscopy, energy dispersive X-ray and atomic force microscopy. The obtained results displayed a layer of nanofibrils able to complex with copper ions in solution. The response of the obtained biosensor was linear up to 50 μM copper and presented a sensitivity of 0.68 μA cm⁻² μM⁻¹. Moreover, the fabricated sensor could be regenerated to a copper-free state allowing its reutilization.

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Section: Resultssupporting

confidence: 64%

Section: ' Materials and Methodsmentioning

confidence: 99%

Development of an Electrochemical Metal-Ion Biosensor Using Self-Assembled Peptide Nanofibrils

Viguier

Zór

Kasotakis

et al. 2011

ACS Appl. Mater. Interfaces

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“…Carny et al fabricated coaxial gold and silver nanocables by binding metallic NPs onto the self-assembled peptide nanotubes via molecular recognition 442. Dinca et al successfully fabricated 3D structures from amyloid fibrils with potential application in molecular electronics 443,444. Amit et al studied the conductance of the thiophene-containing peptide (2-Thi) (2-Thi) VLKAA under a range of humidity conditions 445.…”

Section: Various Applications Of Amyloid-based Hybrid Nanomaterialsmentioning

confidence: 99%

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

et al. 2017

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Self-assembled peptide and protein amyloid nanostructures have traditionally been considered only as pathological aggregates implicated in human neurodegenerative diseases. In more recent times, these nanostructures have found interesting applications as advanced materials in biomedicine, tissue engineering, renewable energy, environmental science, nanotechnology and material science, to name only a few fields. In all these applications, the final function depends on: (i) the specific mechanisms of protein aggregation, (ii) the hierarchical structure of the protein and peptide amyloids from the atomistic to mesoscopic length scales and (iii) the physical properties of the amyloids in the context of their surrounding environment (biological or artificial). In this review, we will discuss recent progress made in the field of functional and artificial amyloids and highlight connections between protein/peptide folding, unfolding and aggregation mechanisms, with the resulting amyloid structure and functionality. We also highlight current advances in the design and synthesis of amyloid-based biological and functional materials and identify new potential fields in which amyloid-based structures promise new breakthroughs.

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“…LIFT has also been applied to the deposition of other biological compounds which do not correspond exactly to biomolecules, but which are nevertheless of great interest in medicine and biology, such as peptides, and more specifically amyloid peptides, which find great use in cell‐growth studies. Similarly, liposomes are also very interesting structures with attractive applications as drug carriers and in biological sensing.…”

Section: Applicationsmentioning

confidence: 99%

Laser‐Induced Forward Transfer: Fundamentals and Applications

Serra

Piqué

2018

Adv Materials Technologies

269

191

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Laser‐induced forward transfer (LIFT) is a digital printing technique that uses a pulsed laser beam as the driving force to project material from a donor thin film toward the receiving substrate whereon that material will be finally deposited as a voxel. This working principle allows LIFT to operate with both solid and liquid donor films, which provides the technique with an unprecedented broad spectrum of printable materials, and thus makes it very competitive over other digital technologies, like inkjet printing. It is not only that LIFT can access a much wider range of ink viscosities and loading particle sizes; the possibility of printing from solid films allows the single‐step printing of multilayers and entire devices, and even makes possible 3D printing. This versatility translates, in turn, into a broad field of applications, from graphics production to printed electronics, from the fabrication of chemical sensors to tissue engineering. This monograph provides an extensive review of the LIFT technique, from its origins to the most recent achievements, focusing on the fundamental aspects of both its working principle and transfer dynamics, as well as on its broad range of applications.

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Fabrication of amyloid peptide micro‐arrays using laser‐induced forward transfer and avidin‐biotin mediated assembly

Cited by 8 publications

References 24 publications

Development of an Electrochemical Metal-Ion Biosensor Using Self-Assembled Peptide Nanofibrils

Development of an Electrochemical Metal-Ion Biosensor Using Self-Assembled Peptide Nanofibrils

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

Laser‐Induced Forward Transfer: Fundamentals and Applications

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