Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 3, Issue 8, Pages 1476-1480Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b411555b
Keywords
-
Categories
Funding
- Biotechnology and Biological Sciences Research Council [EGA17763] Funding Source: Medline
- Biotechnology and Biological Sciences Research Council [BB/C510824/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/D023335/1, EP/D023343/1, GR/T26542/01] Funding Source: researchfish
Ask authors/readers for more resources
The interaction between synthetic glycoplymers bearing beta-D-galactose side groups and the lectin peanut agglutinin (PNA) was investigated by UV-difference spectroscopy and isothermal titration calorimetry (ITC). UV-difference spectroscopy indicated that the polymer lectin interaction was stronger than that between PNA and either the corresponding monomer, D-galactose or D-lactose. The thermodynamics of binding (K, Delta G, Delta H, Delta S and n) were determined from ITC data by fitting with a two-site, non-cooperative binding model. It was found that the glycopolymer displayed around a 50 times greater affinity for the lectin than the parent carbohydrate, and around 10 times greater than the monomer, on a valency-corrected basis. Binding was found to be entropically driven, and was accompanied by aggregation and precipitation of protein molecules. Furthermore, interesting differences between polymers prepared either from deacetylated monomers, or by deacetylation of pre-formed polymers, were found.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available