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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Shiffer K,Hawgood S,Haagsman HP,Benson B,Clements JA,Goerke Jdoi
10.1021/bi00053a026subject
Has Abstractpub_date
1993-01-19 00:00:00pages
590-7issue
2eissn
0006-2960issn
1520-4995journal_volume
32pub_type
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