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Biophysical Journal 85:3928-3934 (2003)
© 2003 The Biophysical Society

Ultrasonic Studies of Alcohol-Induced Transconformation in ß-Lactoglobulin: The Intermediate State

S. Kanjilal *, N. Taulier {dagger}, J.-Y. Le Huérou *, M. Gindre *, W. Urbach {ddagger} and M. Waks *

* Laboratoire d'Imagerie Paramétrique, Université Pierre et Marie Curie, Paris, France; {dagger} Faculty of Pharmacy, University of Toronto, Toronto, Ontario, Canada; and {ddagger} Laboratoire de Physique Statistique, Ecole Normale Supérieure, Paris, France

Correspondence: Address reprint requests to Marcel Waks, Laboratoire d'Imagerie Paramétrique, UMR 7623 CNRS, Université Pierre et Marie Curie, 15 rue de l'Ecole de Médecine, 75270 Paris cedex 06, France. Tel.: 33-14-441-4976; Fax: 33-14-633-5673; E-mail: marcelwaks{at}lip.bhdc.jussieu.fr.

In mixed alcohol-water solvents, bovine ß-lactoglobulin undergoes a cooperative transition from ß-sheet to a high {alpha}-helix content conformer. We report here the characterization of ß-lactoglobulin by compressibility and spectroscopy measurements during this transconformation. Both the volume and compressibility increase as a function of alcohol concentration, up to maximal values which depend on the chemical nature of the three alcohols used: hexafluoroisopropanol, trifluoroethanol, and isopropanol. The order of effectiveness of alcohols in inducing the compressibility transition is identical to that previously reported for circular dichroism and thus independent of the observation technique. The highly cooperative sigmoidal curves found by compressibility determination match closely those obtained by circular dichroism at 222 nm, indicating a correlation between the two phenomena measured by the two different techniques. The presence of an equilibrium intermediate form was shown by the interaction of ß-lactoglobulin with 8-anilino-1-naphthalene sulfonic acid, a probe widely used to detect molten-globule states of proteins. It was correlated with the plateau region of the volume curves and with the inflexion points of the sigmoidal compressibility curves. Ultrasound characterization of proteins can be carried out in optically transparent or nontransparent media.




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