Kinetic and structural characterisation of adsorption induced unfolding of bovine & alpha;-lactalbumin

M.F.M. Engel, C.P.M. Van Mierlo, A.J.W.G. Visser

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Abstract

Conformational changes of bovine α-lactalbumin induced by adsorption on a hydrophobic interface are studied by fluorescence and circular dichroism spectroscopy. Adsorption of bovine α-lactalbumin on hydrophobic polystyrene nanospheres induces a non-native state of the protein, which is characterized by preserved secondary structure, lost tertiary structure, and release of calcium. This partially denatured state therefore resembles a molten globule state, which is an intermediate in the folding of bovine α-lactalbumin. Stopped-flow fluorescence spectroscopy reveals two kinetic phases during adsorption with rate constants k
Original languageEnglish
Pages (from-to)10922-10930
JournalJournal of Biological Chemistry
Volume277
DOIs
Publication statusPublished - 2002

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