Binding of divalent metal ions to 1–25 β-caseinophosphopeptide: An isothermal titration calorimetry study

Autor: Jean-Michel Girardet, Laurent Miclo, Faiza Zidane, Catherine Corbier, Céline Cakir-Kiefer, Aurélie Matéos, Sophie Rahuel-Clermont
Přispěvatelé: Unité de Recherches Animal et Fonctionnalités des Produits Animaux (URAFPA), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA), Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), Centre National de la Recherche Scientifique (CNRS)-Université de Lorraine (UL)
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Phosphopeptides
030309 nutrition & dietetics
Metal ion transport
Cations
Divalent
Metal ions in aqueous solution
[SDV]Life Sciences [q-bio]
Inorganic chemistry
chemistry.chemical_element
Peptide
Zinc
Calorimetry
01 natural sciences
Intestinal absorption
Analytical Chemistry
03 medical and health sciences
Magnesium
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biochemistry [q-bio.BM]
ComputingMilieux_MISCELLANEOUS
chemistry.chemical_classification
0303 health sciences
010401 analytical chemistry
Caseins
Isothermal titration calorimetry
General Medicine
Hydrogen-Ion Concentration
Peptide Fragments
0104 chemical sciences
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biomolecules [q-bio.BM]
chemistry
Intestinal Absorption
Metals
Thermodynamics
Calcium
Absorption (chemistry)
[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
Food Science
Protein Binding
Zdroj: Food Chemistry
Food Chemistry, Elsevier, 2012, 132 (1), pp.391-398. ⟨10.1016/j.foodchem.2011.11.006⟩
ISSN: 0308-8146
DOI: 10.1016/j.foodchem.2011.11.006⟩
Popis: To better understand the mechanism of metal ion transport through the gastrointestinal tract to their absorption sites, isothermal titration calorimetry (ITC) was used to investigate the binding of dicationic metals to β-CN(1-25)4P, a β-casein tetraphosphorylated peptide. ITC technology was found suitable for studying weak bonds between metal ions and phosphopeptides and provided a direct means of thermodynamic and stoichiometric characterisation of complex formation. Thus, one mole of β-CN(1-25)4P binds two moles of Ca(2+), Mg(2+) or Zn(2+) under experimental conditions close to those of the ileum (pH 8, 37°C), with rather low binding affinity constants (K=4900-11,200M(-1)). These low affinities should facilitate the release of metal ions during intestinal absorption. By contrast, Cu(2+) did not bind to β-CN(1-25)4P at pH 8, despite its reported significant affinity towards β-casein and the 1-25 peptide at near-neutral pH.
Databáze: OpenAIRE
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