Journal
COLLOID AND POLYMER SCIENCE
Volume 292, Issue 11, Pages 2765-2774Publisher
SPRINGER
DOI: 10.1007/s00396-014-3319-4
Keywords
BLES; Fbg; AFM; DSC; FTIR; Raman
Categories
Funding
- Grants-in-Aid for Scientific Research [25790020, 26350534] Funding Source: KAKEN
Ask authors/readers for more resources
Lung surfactant (LS), a lipid-protein mixture responsible for alveolar stability, is inhibited by serum proteins leaked into the lungs in disease. Interaction of bovine lipid extract surfactant (BLES), a clinical replacement lung surfactant, with serum protein fibrinogen (Fbg) was studied employing various structural and biophysical techniques in adsorbed films and bulk bilayer dispersions. Surface tension area isotherms of the adsorbed films revealed the suppression of interfacial activity of BLES by Fbg (adsorption and surface tension reduction). Fbg, predominantly associated with the fluid phase of BLES films, resulted in the aggregation of the gel lipid domains as evidenced by atomic force microscopy. BLES bilayer dispersion showed phase transition from a diffused gel to liquid-crystalline phase in the temperature range 10-35 degrees C as studied by differential scanning calorimetry (DSC). Fbg resulted in the shift of peak to a higher transition temperature for the maximal heat flow (T-max) of BLES dispersions. Combined Raman and FTIR spectral studies of the BLES/Fbg dispersions revealed that Fbg altered the -CH2-, -CH3, and -PO4- vibrational modes of the phospholipids present in BLES, suggesting the condensing and dehydrating effect of the protein on surfactant. Studies suggest that Fbg, by directly interacting with the gel lipids in LS in bulk dispersions, alter the packing of the films formed at the interface, and can be used as a specific model for lung disease.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available