Studies of Highly-Ordered Heterodiantennary Mannose/Glucose-Functionalized Polymers and Concanavalin A Protein Interactions Using Isothermal Titration Calorimetry.

ABSTRACT: Preparations of the highly ordered monoantennary, homofunctional diantennary, and heterofunctional diantennary neoglycopolymers of ?-d-mannose and ?-d-glucose residues were achieved via ring-opening metathesis polymerization. Isothermal titration calorimetry measurements of these synthetic neoglycopolymers with Concanavalin A (Con A), revealed that heterofunctional diantennary architectures bearing both ?-mannose and nonbinding ?-glucose units, poly(Man-Glc), binds to Con A (Ka = 16.1 × 10(6) M(-1)) comparably to homofunctional diantennary neoglycopolymer (Ka = 30 × 10(6) M(-1)) bearing only ?-mannose unit, poly(Man-Man). In addition, poly(Man-Glc) neoglycopolymer shows a nearly 5-fold increasing in binding affinity compared to monoantennary neoglycopolymer, poly(Man). Although the exact mechanism for the high binding affinity of poly(Man-Glc) to Con A is unclear, we hypothesize that the ?-mannose bound to Con A might facilitate interaction of ?-glucose with the extended binding site of Con A due to the close proximity of ?-glucose to ?-mannose residues in the designed polymerizable scaffold.

SUBMITTER: Loka RS 

PROVIDER: S-EPMC4766003 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature