title: The complexity of condensed tannin binding to bovine serum albumin--An isothermal titration calorimetry study.
abstract: Isothermal titration calorimetry was applied to study the binding of purified proanthocyanidin oligomers to bovine serum albumin (BSA). The molecular weight of the proanthocyanidin oligomer had a major impact on its binding to BSA. The calculated change in enthalpy (ΔH) and association constant (Ka) became greater as the oligomer size increased then plateaued at the heptameric oligomer. These results support a model for precipitation of proteins by proanthocyanidin where increased oligomer size enhanced the opportunity for cross linkages between proteins ultimately forming sediment-able complexes. The authors suggest tannin binding to proteins is opportunistic and involves multiple sites, each with a different Ka and ΔH of binding. The ΔH of binding comprises both an endothermic hydrophobic interaction and exothermic hydrogen bond component. This suggests the calculated entropy value (ΔS) for tannin-protein interactions is subject to a systematic error and should be interpreted with caution.
authors.affiliation: Department of Economic Development, Jobs, Transport and Resources, Victoria, PO Box 905, Mildura, VIC 3502, Australia. Electronic address: rachel.kilmister@ecodev.vic.gov.au.
authors.forename: Rachel L
authors.initials: RL
authors.lastname: Kilmister
authors.affiliation: Department of Economic Development, Jobs, Transport and Resources, Victoria, PO Box 905, Mildura, VIC 3502, Australia.
authors.forename: Peta
authors.initials: P
authors.lastname: Faulkner
authors.affiliation: Department of Economic Development, Jobs, Transport and Resources, Victoria, PO Box 905, Mildura, VIC 3502, Australia.
authors.forename: Mark O
authors.initials: MO
authors.lastname: Downey
authors.affiliation: Department of Chemical and Biological Engineering, ChELSI Institute, University of Sheffield, Sheffield S1 3JD, England, United Kingdom.
authors.forename: Samuel J
authors.initials: SJ
authors.lastname: Darby
authors.affiliation: Department of Chemical and Biological Engineering, ChELSI Institute, University of Sheffield, Sheffield S1 3JD, England, United Kingdom.
authors.forename: Robert J
authors.initials: RJ
authors.lastname: Falconer
mesh_terms: D000818:Animals; D002151:Calorimetry / Q000379:methods*; D002417:Cattle; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D044945:Proanthocyanidins / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013634:Tannins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D044945:Proanthocyanidins; D013634:Tannins; C013221:proanthocyanidin; D012710:Serum Albumin, Bovine
keywords: Hydrogen bonding; Hydrophobic interaction; Oligomer; Proanthocyanidin; Thermodynamics