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Title: Comparison of the enthalpy state of vesicles of different size by their interaction with alpha-lactalbumin
Authors: van Cauwelaert, R ×
Hanssens, Ignace
Herreman, Willy
van Ceunebroeck, J C
Baert, O
Berghmans, Hugo #
Issue Date: Jan-1983
Series Title: Biochimica et Biophysica Acta vol:727 issue:2 pages:273-84
Abstract: The characteristics of small unilamellar, large unilamellar and large multilamellar vesicles of dimyristoylphosphatidylcholine and their interaction with alpha-lactalbumin are compared at pH 4. (1) By differential scanning calorimetry and from steady-state fluorescence anisotropy data of the lipophilic probe 1,6-diphenyl-1,3,5-hexatriene it is shown that the transition characteristics of the phospholipids in the large unilamellar vesicles resemble more those of the multilamellar vesicles than of the small unilamellar vesicles. (2) The size and composition of the lipid-protein complex formed with alpha-lactalbumin around the transition temperature of the lipid are independent of the vesicle type used. Fluorescence anisotropy data indicate that in this complex the motions of the lipid molecules are strongly restricted in the presence of alpha-lactalbumin. (3) The previous data and a comparison of the enthalpy changes, delta H, of the interaction of the three vesicle types with alpha-lactalbumin allow us to derive that the enthalpy state of the small unilamellar vesicles just below 24 degrees C is about 24 kJ/mol lipid higher than the enthalpy state of both large vesicle types at the same temperature. The abrupt transition from endothermic to exothermic delta H values around 24 degrees C for large vesicles approximates the transition enthalpy of the pure phospholipid.
ISSN: 0006-3002
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Faculty of Science, Campus Kulak Kortrijk
Molecular Imaging and Photonics
× corresponding author
# (joint) last author

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