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  • Title: Lung surfactant proteins, SP-B and SP-C, alter the thermodynamic properties of phospholipid membranes: a differential calorimetry study.
    Author: Shiffer K, Hawgood S, Haagsman HP, Benson B, Clements JA, Goerke J.
    Journal: Biochemistry; 1993 Jan 19; 32(2):590-7. PubMed ID: 8422370.
    Abstract:
    The ability of the low molecular weight lung surfactant-associated proteins, SP-B and SP-C, to alter the thermotropic properties of synthetic multilamellar vesicles was tested using differential scanning calorimetry (DSC). The presence of either SP-B or SP-C in dipalmitoylphosphatidylcholine (DPPC) or dipalmitoylphosphatidylglycerol (DPPG) multilamellar vesicles broadened the DSC thermogram and reduced the enthalpy of transition in a concentration-dependent manner. With both proteins, the temperature at which the peak of the phase transition (Tm) was detected was shifted to a higher value. The increase in Tm caused by both proteins was greater with DPPG than DPPC. We have interpreted these results as implying the presence of a protein-perturbed domain of lipid. Both SP-B and SP-C were found to influence the surface activity of the phospholipids in a concentration-dependent fashion. We speculate that instability of lipid packing predicted to occur at protein-created lipid domain boundaries may be important for the expression of surface activity in pulmonary surfactant.
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