Synthesis of Mannosylated Glycodendrimers and Evaluation against BC2L-A Lectin from Burkholderia Cenocepacia.

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 sol. 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 prepd. and their interactions with BC2L-A were thermodynamically characterized by isothermal titrn. calorimetry. The results show that a 24-valent structure binds to BC2L-A at nanomolar concn., which makes this compd. the highest affinity monodisperse ligand for this lectin. [on SciFinder(R)]

Références

Titre
Synthesis of Mannosylated Glycodendrimers and Evaluation against BC2L-A Lectin from Burkholderia Cenocepacia.
Type de publication
Article de revue
Année de publication
2017
Revue
Chempluschem
Volume
82
Pagination
390–398
ISSN
2192-6506
Soumis le 12 avril 2018