Clémence CheignonInstitut Pluridisciplinaire Hubert Curien | IPHC · Department of analytical sciences
Clémence Cheignon
PhD in analytical chemistry
About
23
Publications
5,733
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1,633
Citations
Citations since 2017
Introduction
Additional affiliations
September 2019 - present
September 2019 - present
September 2018 - August 2019
University of Strasbourg
Position
- Research Assistant
Education
September 2013 - November 2016
September 2012 - June 2013
Publications
Publications (23)
Oxidative stress that can lead to oxidation of the amyloid-β (Aβ) peptide is considered a key feature in Alzheimer’s disease (AD), influencing the ability of Aβ to assemble into β-sheet rich fibrils that are commonly found in senile plaques of AD patients. The present study aims at investigating the fallouts of Aβ oxidation on the assembly properti...
A major challenge in nanomedicine is designing nanoplatforms (NPFs) to selectively target abnormal cells to ensure early diagnosis and targeted therapy. Among developed NPFs, iron oxide nanoparticles (IONPs) are good MRI contrast agents and can be used for therapy by hyperthermia and as radio-sensitizing agents. Active targeting is a promising meth...
Due to their exceptional luminescent properties, lanthanide (Ln) complexes represent a unique palette of probes in the spectroscopic toolkit. Their extremely weak brightness due to forbidden Ln electronic transitions can be overcome by indirect dye-sensitization from the antenna effect brought by organic ligands. Despite the improvement brought by...
The surface coordination of p ‐sulfonato‐ (C[4]), p ‐sulfonatothia‐ (SC[4]) and p ‐sulfonato‐sulfoxocalix[4]arene (SO 2 C[4]) on La 0.9 Tb 0.1 F 3 nanoparticles (TbNP) was investigated by UV‐Vis absorption and luminescence spectroscopies. SO 2 C[4] displayed the strongest affinity towards the NPs and a significant antenna effect leading to observat...
Novel trifunctional ligands enable simultaneous bioconjugation (e.g., to antibodies), attachment to nanoparticle surfaces, and photosensitization of Tb ions, affording ultrabright biofunctionalized Tb nanoparticles. These luminescent nanoparticle bioconjugates were successfully implemented in time‐gated FRET spectroscopy and luminescence microscopy...
Lanthanide‐doped nanoparticles (LnNPs) have become an important class of fluorophores for advanced biosensing and bioimaging. LnNPs that are photosensitized by surface‐attached antenna ligands can possess exceptional brightness. However, their functional bioconjugation remains an important challenge for their translation into bioanalytical applicat...
In the search of an alternative strategy to radioactivity measurement conventionally performed to probe receptor-ligand interactions in pharmacological assays, we demonstrated that selenium labeling of the studied ligand combined with elemental mass spectrometry was as efficient and robust as the reference method but devoid of its environmental and...
Oxidative stress is known to play an important role in the pathogenesis of a number of diseases. In particular, it is linked to the etiology of Alzheimer's disease (AD), an age-related neurodegenerative disease and the most common cause of dementia in the elderly. Histopathological hallmarks of AD are intracellular neurofibrillary tangles and extra...
Alzheimer’s Disease (AD) is characterized by the deposition of amyloid plaques, mainly composed of aggregates of the Amyloid-β peptide (Aβ). There are evidences of oxidative damages on biomolecules and on Aβ in vivo, suggesting a link between oxidative stress and AD. The dyshomeostasis of redox-active metal ions observed in AD and in particular the...
Metal-catalyzed oxidation of Aβ and ROS production: an Alzheimer's Disease story Identification of key structural features of the Aβ/copper state responsible for ROS production.
Oxidative stress is linked to the etiology of Alzheimer’s disease (AD), the most common cause of dementia in the elderly. Redox active metal ions such as copper catalyze the production of Reactive Oxygen Species (ROS) when bound to the amyloid-β (Aβ) peptide encountered in AD. We propose that this reaction proceeds through a low-populated Cu-Aβ sta...
Alzheimer's Disease (AD) is the most frequent for of dementia in the elderly. A hallmark of AD is the extracellular formation of senile plaques in the brain of AD subjects, composed of the Amyloid-ß peptide (Aß) under aggregated form with metal ions such as copper ions. Aß can form a complex with copper ions, able to catalyze reactive oxygen specie...
In the context of Alzheimer's disease (AD), the production of HO center dot by copper-amyloid beta (Ab) in the presence of ascorbate is known to be deleterious for the A beta peptide itself and also for the surrounding molecules, thus establishing a direct link between AD and oxidative stress. The metal-catalyzed oxidation (MCO) of A beta primarily...
Evaluation of the pro versus antioxidant activity of ascorbate regarding Cu(Aβ) induced reactive oxygen species production in the context of Alzheimer’s disease shows that a protective activity can only be observed at high ascorbate concentration for exogenous molecules but not for the amyloid-β peptide itself.
In the AD context, to study the effects of ascorbate concentration on the oxidation of surrounding biomolecules.
Monitoring of the oxidation of the 3-CCA (that mimic surrounding molecule) in fluorescence spectroscopy.
Almost 36 million people in the world are affected by dementia, most suffering from Alzheimer's disease (AD). One of the feature of AD is the formation of senile plaques in brain, mainly composed of the 40/42-residue Beta-Amyloid peptide (Aβ). It is known that the Aβ peptide is present in soluble form in healthy brain and found aggregated in Alzhei...
Questions
Question (1)
I would like to use cyanogen bromide to cleave a peptide after methionine residues. Numerous studies have deal with this use and all of them have a lyophilization step (or vacuum step) at the end of the reaction in order to remove the excess of cyanogen bromide. However, none of them explain how they manage to do the lyophilization without spread the BrCN (that is extremely harmfull and goes with the water) in the whole lyophilizer. Does anyone could help me ?
Thanks by advance
