Structural changes of human serum albumin immobilized on chromatographic supports: a high-performance liquid chromatography and Fourier-transform infrared spectroscopy study - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Chromatography B Biomedical Sciences and Applications Année : 2001

Structural changes of human serum albumin immobilized on chromatographic supports: a high-performance liquid chromatography and Fourier-transform infrared spectroscopy study

Résumé

Chiral stationary phases obtained by immobilization of HSA on [C8] and [C18] reversed-phases and on poly(1-vinylimidazole)-coated silica were tested to resolve dl-tryptophan, N-benzoyl-dl-phenylalanine, RS-oxazepam and RS-warfarin racemic mixtures. Parameters of enantioselectivity measured in HPLC are correlated to structural and solvation states for adsorbed HSA, evaluated by FTIR spectroscopy. HSA immobilized on [PVI]-anion-exchangers is highly selective. HSA molecules are not self-associated, only unfolded for a small hydrophobic helix. The HSA-coated reversed-phases have a lower selectivity. Unfolding is larger but the indole-benzodiazepine chiral site is preserved and remains accessible.

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Chimie

Dates et versions

hal-03085276 , version 1 (21-12-2020)

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Citer

M.C Millot, S Servagent-Noinville, N.L Taleb, M.H Baron, M Revault, et al.. Structural changes of human serum albumin immobilized on chromatographic supports: a high-performance liquid chromatography and Fourier-transform infrared spectroscopy study. Journal of Chromatography B Biomedical Sciences and Applications, 2001, 753 (1), pp.101-113. ⟨10.1016/S0378-4347(00)00424-2⟩. ⟨hal-03085276⟩
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