News

Filtrer par
1 2 3 7

Visualisation of hydrogen atoms in a perdeuterated lectin-fucose complex reveals key details of protein-carbohydrate interactions

The pathogenic bacteria attach themselves to the cells which they attack thanks to the sugars present on their membrane. A crucial mechanism to study, because it would help to treat these infections without reinforcing the resistance of the bacteria. To do this, researchers from CERMAV (CNRS), the Laue-Langevin Institute (ILL) and CEITEC (Masaryk University, Czech Republic) have modified a sugar so that it responds to neutron crystallography, a technique that reveals how bacteria cling to sugars. This work, published in the journal Structure, could extend to more complex sugars to better understand different biological phenomena and propose new anti-infectious strategies. Caption: Fucose molecule in the lectin binding site. The blue grid represents the density determined by x-rays and the green grid the density determined by the neutrons around the fucose and the amino acids of the lectin. Hydrogen atoms (here isotope deuterium) are represented by yellow balls. The continuity of the green grid between the fucose and the amino acids allows a direct view of the hydrogen bonds. © L. Gajdos. / Click on the title for more information.

Crystal and molecular structure of V-amylose complexed with ibuprofen

We have published an article in Carbohydrate Polymers about the structure of an inclusion compound prepared by crystallizing amylose in the presence of ibuprofen, a well-known anti-inflammatory drug. Using data from solid-state NMR, and electron and X-ray diffraction, we have proposed a molecular model allowing to locate the ibuprofen guest molecules in the lattice of amylose helices. Click on the title for more information.
S’abonner à la newsletter du laboRecevez chaque semaine les dernières actualités du laboratoire par email.
1 2 3 7