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Marie Carriere’ s thesis defense on January 25th, 2021

Such thesis is entitled "Design, characterization and application of glyconanoparticles in (bio) electrochemistry". It is executed in collaboration with the Département de Chimie Moléculaire (DCM), and the CEntre de Recherches sur les MAcromolécules Végétales (CERMAV) (co-supervised by Redouane BORSALI -Director of Research at CNRS). Click on the title for more information.

Bottom-up Construction of Xylan Nanocrystals in Dimethyl Sulfoxide

In collaboration with Aalto University and VTT (Finland), we developed a new hemicellulose-based nanocrystal composed of crystalline complex of xylan and dimethyl sulfoxide. The detailed structural characterization revealed that the xylan molecules are packed in the nanocrystals with a two-fold helical conformation which is different from the three-fold helical conformation found in the pure xylan crystal. The morphology of nanocrystals was found to be adjustable through changing the crystallization conditions. This work will serve as a starting point to understand the controlled assembly of hemicelluloses to discover their full application potential. Click on the title for more information.

Non‐Carbohydrate Glycomimetics as Inhibitors of Calcium(II)‐binding Lectins

Search for new inhibitors of bacterial infection is a priority for fighting antibiotics resistance, and this is the topic of a french-german ANR-DFG project. We screened for libraries of non-carbohydrate ligands for binding to Pseudomonas aeruginosa calcium-dependent lectins, and identified catechol derivatives as interesting lead. The first co‐crystal structure of a non‐carbohydrate inhibitor in complex with a bacterial lectin clearly demonstrates the catechol mimicking the binding of natural glycosides with LecA. Interstingly, catechol derivatives also bind to human C-type lectins, opening a wide range of applications. Click on the title for more information.

Happy New Year!

Both CNRS and Cermav wish you a happy New Year and all the best for 2021. Click on the title to watch the video.

GAG-DB, the New Interface of the Three-Dimensional Landscape of Glycosaminoglycans

Glycosaminoglycans (GAGs) are complex linear polysaccharides. GAG-DB is a curated database that classifies the three-dimensional features of the six mammalian GAGs (chondroitin sulfate, dermatan sulfate, heparin, heparan sulfate, hyaluronan, and keratan sulfate) and their oligosaccharides complexed with proteins. GAG-DB provides detailed information on GAGs, their bound protein ligands, and features their interactions using several open access applications. Binding covers interactions between monosaccharides and protein monosaccharide units and the evaluation of quaternary structure. Click on the title for more information.
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