Surfactant protein B (SP-B) is an essential component of pulmonary surfactant. Synthetic dimeric SP-B1-25 (SP-B1-25), a peptide based on the N-terminal domain of human SP-B, efficiently mimics the functional properties of SP-B. The authors investigated the optimum lipid composition for SP-B1-25 by comparing the effects of natural lung lavage lipids (NLL), a synthetic equivalent of NLL (synthetic lavage lipids SLL), and a standard lipid mixture (TL) on the activities of SP-B 1-25. Surfactant preparations were formulated by mixing 2 mol% SP-B1-25 in NNL, SLL, and TL. Calfactant, a calf lung lavage extract with SP-B and SP-C, was a positive control and lipids without peptide were negative controls. Minimum surface tension measured on a captive bubble surfactometer was similar for the three SP-B1-25 surfactant preparations and calfactant. The effects on lung function were compared in ventilated, lavaged, surfactant-deficient rats. Oxygenation and lung volumes were consistently higher in rats treated with calfactant and SP-B1-25 in NLL or SLL than in rats treated with SP-B1-25 in TL. Fourier transform infrared spectra observed abnormal secondary conformations for SP-B1-25 in TL as a possible cause for the reduced lung function. Lipid composition plays a crucial role in the in vitro and in vivo functions of SP-B1-25 in surfactant preparations.
Bibliographical noteFunding Information:
This work was supported by grant HL55534 from the National Institutes of Health. The REI Bruker Vector 22 FTIR spectrometer was funded by a grant from the Harbor–UCLA REI Common Use and Replacement Equipment Program. Calfactant (Infasurf) was a generous gift of Ony Inc., Amherst, New York.
- Captive bubble surfactometry
- Dimeric SP-B peptide
- Fourier transform infrared spectroscopy
- Lung function