مؤتمر
Flow-through partial-filling affinity capillary electrophoresis for the detection of weak ligand-target interactions: application to coagulation factor XIIa
| العنوان: | Flow-through partial-filling affinity capillary electrophoresis for the detection of weak ligand-target interactions: application to coagulation factor XIIa |
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| المؤلفون: | Davoine, Clara, Farcas, Elena, Bouckaert, Charlotte, Pochet, Lionel, Fillet, Marianne |
| المساهمون: | CIRM - Centre Interdisciplinaire de Recherche sur le Médicament - ULiège, NARILIS - NAmur Research Institute for LIfe Sciences |
| المصدر: | CIRM-day 2019, Liège, Belgium [BE], 11 décembre 2019 |
| سنة النشر: | 2019 |
| مصطلحات موضوعية: | Affinity capillary electrophoresis (ACE), fragment-based lead discovery (FLDD), coagulation factor XIIa (FXIIa), Life sciences, Biochemistry, biophysics & molecular biology, Human health sciences, Pharmacy, pharmacology & toxicology, Sciences du vivant, Biochimie, biophysique & biologie moléculaire, Sciences de la santé humaine, Pharmacie, pharmacologie & toxicologie |
| الوصف: | Coagulation factor XIIa (FXIIa) is a S1A serine protease implicated in several physiological pathways including the intrinsic coagulation pathway, the kallikrein-kinin system, and the immune response. In the field of thrombosis, anti-FXIIa therapies could answer unmet medical needs such as the safe prevention of thrombosis in patients exposed to blood-contacting devices. The FXIIa inhibition also rises as a therapeutic strategy in patients suffering from hereditary angioedema and as an emerging research field in neuro-inflammatory and neurodegenerative disorders.The FXII or FXIIa inhibitors currently under development include peptides, proteins, antibodies, and RNA-based technologies. In contrast, only a few data regarding the design of synthetic small molecular-weight inhibitors of FXIIa are available. Our team previously developed 3-carboxamido-benzopyrans and highlighted that aromatic guanidine is an attractive starting point. To facilitate chemical exploration, we decided to apply a fragment-based lead discovery approach (FBLD). However, the success of this approach rests on the ability to develop bioassays that are able to detect affinity in the µM-mM range.For this purpose, we develop a flow-through partial-filling affinity capillary electrophoresis designed to screen positively-charged molecules against FXIIa at physiological pH. Development of new compounds targeting coagulation factor XIIa using innovative microfluidic assays in the context of fragment-based drug discovery |
| نوع الوثيقة: | conference poster not in proceedings http://purl.org/coar/resource_type/c_18co conferencePoster |
| اللغة: | English |
| URL الوصول: | https://orbi.uliege.be/handle/2268/242803 |
| رقم الأكسشن: | edsorb.242803 |
| قاعدة البيانات: | ORBi |
| الوصف غير متاح. |