Comparison of the enthalpy state of vesicles of different size by their interaction with alpha-lactalbumin.
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.
D002152:Calorimetry, Differential Scanning; D004134:Dimyristoylphosphatidylcholine; D005454:Fluorescence Polarization; D006863:Hydrogen-Ion Concentration; D007768:Lactalbumin; D008081:Liposomes; D008854:Microscopy, Electron; D010713:Phosphatidylcholines; D013329:Structure-Activity Relationship
D008081:Liposomes; D010713:Phosphatidylcholines; D007768:Lactalbumin; D004134:Dimyristoylphosphatidylcholine