Charlotte Rimbault

ORCID: 0000-0002-4760-8430
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About
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Research Areas
  • Venomous Animal Envenomation and Studies
  • Toxin Mechanisms and Immunotoxins
  • X-ray Diffraction in Crystallography
  • Biochemical and Structural Characterization
  • Crystallization and Solubility Studies
  • Monoclonal and Polyclonal Antibodies Research
  • Radiopharmaceutical Chemistry and Applications
  • Cellular transport and secretion
  • Advanced Fluorescence Microscopy Techniques
  • Protein Structure and Dynamics
  • Hippo pathway signaling and YAP/TAZ
  • Cell Image Analysis Techniques
  • Glycosylation and Glycoproteins Research
  • Nicotinic Acetylcholine Receptors Study
  • Synthesis and biological activity
  • Medical Imaging Techniques and Applications
  • Synthesis and Biological Evaluation
  • Rabies epidemiology and control
  • Photoreceptor and optogenetics research
  • Photosynthetic Processes and Mechanisms
  • Synthesis and Characterization of Heterocyclic Compounds
  • Chemical Synthesis and Analysis
  • Synthesis and Reactivity of Heterocycles
  • Advanced Biosensing Techniques and Applications
  • RNA Research and Splicing

Université de Bordeaux
2013-2024

Institut Interdisciplinaire de Neuroscience
2016-2024

Centre National de la Recherche Scientifique
2013-2024

Technical University of Denmark
2020-2024

Despite the constant advances in fluorescence imaging techniques, monitoring endogenous proteins still constitutes a major challenge particular when considering dynamics studies or super-resolution imaging. We have recently evolved specific protein-based binders for PSD-95, main postsynaptic scaffold at excitatory synapses. Since synthetic recombinant recognize epitopes not directly involved target protein activity, we consider them here as tools to develop PSD-95 probes. After confirming...

10.7554/elife.69620 article EN cc-by eLife 2024-01-03

Recombinantly produced biotherapeutics hold promise for improving the current standard of care snakebite envenoming over conventional serotherapy. Nanobodies have performed well in clinic, and context antivenom, they shown ability to neutralize long α-neurotoxins

10.1021/acs.bioconjchem.2c00220 article EN cc-by Bioconjugate Chemistry 2022-07-23

Abstract Designing highly specific modulators of protein-protein interactions (PPIs) is especially challenging in the context multiple paralogs and conserved interaction surfaces. In this case, direct generation selective competitive inhibitors hindered by high similarity within evolutionary-related protein interfaces. We report here a strategy that uses semi-rational approach to separate modulator design into two functional parts. first achieve specificity toward region outside interface...

10.1038/s41467-019-12528-4 article EN cc-by Nature Communications 2019-10-04

Three-finger toxins (3FTxs) have traditionally been obtained via venom fractionation of whole venoms from snakes. This method often yields functional toxins, but it can be difficult to obtain pure isoforms, as is challenging separate the many different with similar physicochemical properties that generally exist in venoms. issue circumvented use recombinant expression. However, achieving correct disulfide bond formation and requires extensive optimization expression purification methods...

10.1016/j.toxicon.2024.107613 article EN cc-by Toxicon 2024-01-11

Phage display technology is a powerful tool for selecting monoclonal antibodies against diverse set of antigens. Within toxinology, however, it remains challenging to generate many animal toxins, as they are difficult obtain from venom. Recombinant toxins have been proposed solution overcome this challenge, but so far, few used antigens neutralizing antibodies. Here, we describe the recombinant expression α-cobratoxin in E. coli and its successful application an antigen phage selection...

10.1016/j.nbt.2023.04.002 article EN cc-by New Biotechnology 2023-04-08

Recycling IgG antibodies bind to their target antigen at physiological pH in the blood stream and release them upon endocytosis when levels drop, allowing be recycled into circulation via FcRn-mediated cellular pathways, while antigens undergo lysosomal degradation. This enables recycling achieve comparable therapeutic effect lower doses than non-recycling counterparts. The development of such is typically achieved by histidine doping variable regions or performing vitro antibody selection...

10.1002/pro.4821 article EN cc-by Protein Science 2023-10-28

ABSTRACT Despite the constant advances in fluorescence imaging techniques, monitoring endogenous proteins still constitutes a major challenge particular when considering dynamics studies or super-resolution imaging. We have recently evolved specific protein-based binders for PSD-95, main postsynaptic scaffold at excitatory synapses. Since synthetic recognize epitopes not directly involved target protein activity, we consider them here as tools to develop PSD-95 probes. After confirming their...

10.1101/2021.04.07.438431 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2021-04-08

Abstract Recycling antibodies can bind to their target antigen at neutral pH in the blood stream and release them upon endocytosis when levels drop, allowing be recycled into circulation via FcRn-mediated pathway, while antigens undergo lysosomal degradation. This enables recycling achieve same therapeutic effect lower doses than non-recyclable counterparts. The development of such is typically achieved by histidine doping variable regions specific or performing vitro antibody selection...

10.1101/2023.05.08.539834 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2023-05-09

In the crystal structure of title compound, C16H24N4O4, mol-ecules are linked by N-H⋯O hydrogen bonds between carbonyl groups carbamoyl and amido functional amino groups, N-H⋯N group pyridine ring, forming two-dimensional networks parallel to ab plane.

10.1107/s1600536813024598 article EN Acta Crystallographica Section E Structure Reports Online 2013-09-11
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