Synthesis of Mannosylated Glycodendrimers and Evaluation against BC2L‐A Lectin from Burkholderia Cenocepacia. Issue 3 (14th December 2016)

• Record Type: Journal Article
• Authors: Pifferi, Carlo; Goyard, David; Gillon, Emilie; Imberty, Anne; Renaudet, Olivier
• Is Part Of: ChemPlusChem. Volume 82:Issue 3(2017)
• Page Start: 390
• Page End: 398
• Publication Date: 2016-12-14
• Subjects: chemoselectivity -- dendrimers -- glycoconjugates -- lectins -- multivalency; Chemistry -- Periodicals; 540.5
• DOI: 10.1002/cplu.201600569
• Languages: English
• ISSNs: 2192-6506

Abstract

Abstract: Chronic colonization of lungs by opportunist bacteria is the major cause of mortality for cystic fibrosis patients. Among these pathogens, Burkholderia cenocepacia is responsible for cepacia syndrome, a deadly exacerbation of infection that is the main cause of poor outcomes of lung transplantation. This bacterium contains three soluble carbohydrate‐binding proteins, including the B. cenocepacia lectin A (BC2L‐A), which is proposed to bind to oligomannose‐type N ‐glycan structures to adhere to host tissues. In this work, several mannosylated glycoclusters and glycodendrimers with valencies ranging from four to 24 were prepared and their interactions with BC2L‐A were thermodynamically characterized by isothermal titration calorimetry. The results show that a 24‐valent structure binds to BC2L‐A at nanomolar concentration, which makes this compound the highest affinity monodisperse ligand for this lectin. Abstract : Hold on tight ! The synthesis of mannosylated glycoclusters and glycodendrimers with valencies ranging from four to 24 and the thermodynamic characterization of their interactions with the bacterial lectin BC2L‐A by isothermal titration calorimetry are described. It is shown that a 24‐valent structure binds to BC2L‐A at nanomolar concentration, making this the highest affinity monodisperse ligand for this lectin.