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 α-d-mannose and β-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 β-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 β-glucose with the extended binding site of Con A due to the close proximity of β-glucose to α-mannose residues in the designed polymerizable scaffold.

journal_name

Biomacromolecules

journal_title

Biomacromolecules

authors

Loka RS,McConnell MS,Nguyen HM

doi

10.1021/acs.biomac.5b01380

subject

Has Abstract

pub_date

2015-12-14 00:00:00

pages

4013-4021

issue

12

eissn

1525-7797

issn

1526-4602

journal_volume

16

pub_type

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