2008
DOI: 10.1039/b805406c
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Interactions of aluminium hydrolytic species with biomolecules

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Cited by 20 publications
(28 citation statements)
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“…Our research aims to understand how charge, morphology and the structure of the aluminium species influence how they interact with proteins [50,51]. Our research aims to understand how charge, morphology and the structure of the aluminium species influence how they interact with proteins [50,51].…”
Section: Towards Improved Aluminium-containing Materialsmentioning
confidence: 99%
“…Our research aims to understand how charge, morphology and the structure of the aluminium species influence how they interact with proteins [50,51]. Our research aims to understand how charge, morphology and the structure of the aluminium species influence how they interact with proteins [50,51].…”
Section: Towards Improved Aluminium-containing Materialsmentioning
confidence: 99%
“…40,97 Since both G-12 and GT-16 have no acidic amino acid residues, the bound COO À most probably arose from the C-terminus of these peptides.…”
mentioning
confidence: 99%
“…Yu et al [231] used 2D NIR to study the pH-induced secondary structure change and binding interaction between bovine serum albumin and famotidine, a histamine H 2 -receptor antagonist. Deschaume et al [236] used 2D IR to study the interactions between polycationic aluminum species and lysozyme or bovine serum albumin and bioinorganic assembly formation. Wang et al [239] used 2D fluorescence to study the binding of pyridazin-3(2H)-one derivative to human serum albumin.…”
Section: Proteins and Peptidesmentioning
confidence: 99%
“…2D IR was used by Deschaume et al [236] to study the interactions between polycationic aluminum species and lysozyme or bovine serum albumin. Concentration of aluminum species was used as the perturbation.…”
Section: Compositionmentioning
confidence: 99%