Studies of Highly-Ordered Heterodiantennary Mannose/Glucose-Functionalized Polymers and Concanavalin A Protein Interactions Using Isothermal Titration Calorimetry.
Biomacromolecules
; 16(12): 4013-4021, 2015 Dec 14.
Article
in En
| MEDLINE
| ID: mdl-26580410
ABSTRACT
Preparations of the highly ordered monoantennary, homofunctional diantennary, and heterofunctional diantennary neoglycopolymers of α-d-mannose and ß-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 α-mannose and nonbinding ß-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 α-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 α-mannose bound to Con A might facilitate interaction of ß-glucose with the extended binding site of Con A due to the close proximity of ß-glucose to α-mannose residues in the designed polymerizable scaffold.
Full text:
1
Database:
MEDLINE
Main subject:
Concanavalin A
/
Glucose
/
Mannose
Language:
En
Year:
2015
Type:
Article