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Sébastien Vidal

Researcher at Claude Bernard University Lyon 1

Publications -  162
Citations -  5018

Sébastien Vidal is an academic researcher from Claude Bernard University Lyon 1. The author has contributed to research in topics: Glycogen phosphorylase & Lectin. The author has an hindex of 35, co-authored 159 publications receiving 4476 citations. Previous affiliations of Sébastien Vidal include University of California, Los Angeles & University of Montpellier.

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Sweet carbon nanostructures: carbohydrate conjugates with carbon nanotubes and graphene and their applications

TL;DR: This review will highlight the synthetic strategies that have been reported for the covalent and noncovalent functionalization of carbon nanostructures with carbohydrates, as well as their applications in biosensing and biomedicine.
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Fucosylated pentaerythrityl phosphodiester oligomers (PePOs): automated synthesis of DNA-based glycoclusters and binding to Pseudomonas aeruginosa lectin (PA-IIL).

TL;DR: The synthesis of propargylated pentaerythrityl phosphodiester oligomers (PePOs) was achieved using a DNA synthesizer with a bis-propargylator-based phosphoramidite and the IC50 values measured are 10-20 times better than for monovalent l-fucose and denotate for a "macromolecular" effect rather than a "cluster" effect.
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Nanoelectronic detection of lectin-carbohydrate interactions using carbon nanotubes.

TL;DR: Fluorescence microscopy, atomic force microscope, UV-vis-NIR spectroscopy, and several control measurements confirmed the NTFET response to selective interactions between carbohydrates and lectins, and no significant change in the device characteristics was observed when the devices were exposed to other lectins with different specificity.
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Rational Design and Synthesis of Optimized Glycoclusters for Multivalent Lectin–Carbohydrate Interactions: Influence of the Linker Arm

TL;DR: Improved and unprecedented affinities for one of the monovalent probes (K(d)=5.8 μM) and also for a number of the tetravalent compounds that provide several new nanomolar ligands for this tetrameric lectin.