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Issue 8, 2005
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Investigation of the interaction between peanut agglutinin and synthetic glycopolymeric multivalent ligands

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Abstract

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.

Graphical abstract: Investigation of the interaction between peanut agglutinin and synthetic glycopolymeric multivalent ligands

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Publication details

The article was received on 27 Jul 2004, accepted on 21 Feb 2005 and first published on 07 Mar 2005


Article type: Paper
DOI: 10.1039/B411555B
Citation: Org. Biomol. Chem., 2005,3, 1476-1480
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    Investigation of the interaction between peanut agglutinin and synthetic glycopolymeric multivalent ligands

    M. Ambrosi, N. R. Cameron, B. G. Davis and S. Stolnik, Org. Biomol. Chem., 2005, 3, 1476
    DOI: 10.1039/B411555B

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