TY - JOUR
T1 - Investigation of the interaction between peanut agglutinin and synthetic glycopolymeric multivalent ligands
AU - Ambrosi, Moira
AU - Cameron, Neil R.
AU - Davis, Benjamin G.
AU - Stolnik, Snjezana
PY - 2005/4/21
Y1 - 2005/4/21
N2 - The interaction between synthetic glycoplymers bearing β-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, ΔG, ΔH, ΔS 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.
AB - The interaction between synthetic glycoplymers bearing β-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, ΔG, ΔH, ΔS 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.
UR - http://www.scopus.com/inward/record.url?scp=18444401403&partnerID=8YFLogxK
U2 - 10.1039/b411555b
DO - 10.1039/b411555b
M3 - Article
C2 - 15827644
AN - SCOPUS:18444401403
SN - 1477-0520
VL - 3
SP - 1476
EP - 1480
JO - Organic & Biomolecular Chemistry
JF - Organic & Biomolecular Chemistry
IS - 8
ER -