Pulmonary Surfactant: Physical Chemistry, Physiology, and Replacement

Content-dependent activity of lung surfactant protein B in mixtures with lipids

“…However, surface activity successively increased as SP-B content was incrementally raised to 0.75% by weight relative to phospholipid. The adsorption and dynamic surface tension lowering of PPL/SP-B (0.75%) were only slightly less than CLSE, a highly active surfactant extract containing the complete mix of lipids and hydrophobic proteins from lavaged calf lung surfactant (18,21,33,34,38) (Figs. 1C and 4).…”

“…However, physiological data were consistent with biophysical findings in showing an overall pattern of increasing activity for SL/SP-B mixtures as apoprotein content increased. The excised rat lung model in our experiments has previously been used with success to correlate the pulmonary activity of lung surfactants with their surface activity and inhibition (e.g., 17,21,22,38). The rat lung model has also been shown in multiple studies to respond to the instillation of whole and extracted lung surfactant materials that improve in vivo pulmonary function in other animal models of surfactant deficiency and dysfunction (see Ref.…”

“…The physiological necessity of surfactant in respiratory function has led to extensive research on the biophysics, cell and molecular biology, and physiology of this complex material (11,20,34,38). Although lipids (primarily phospholipids) comprise the great majority of lung surfactant in a quantitative sense, the apoprotein constituents of the surfactant system are highly active and crucial in a functional sense.…”

Molecular interactions of cord factor with dipalmitoylphosphatidylcholine monolayers: Implications for lung surfactant dysfunction in pulmonary tuberculosis

“…During dynamic respiratory cycles, the unsaturated surfactant lipids are extruded into the alveolar subphase from the pulmonary air-aqueous interface and the interfacial surfactant film behaves like a pure DPPC monolayer [30]. Hence, DPPC monolayers closely simulate the surfactant film at the air-aqueous interface and inhibition of DPPC surface activity is also associated with impairment of lung surfactant function in vivo [31].…”

Interactions between hematological derivatives and dipalmitoyl phosphatidyl choline: implications for adult respiratory distress syndrome

“…This could be the result of biophysical/biochemical interactions between surfactant components and blood components that invade the alveoli as a result of capillary damage [3]. Several studies have reported that the plasma proteins especially fibrinogen and albumin may be responsible for inhibiting the surface activity of the lung surfactant during this condition [4,5]. Albumin is the major plasma protein and has been reported to be inhibitory to the adsorption process as well as the dynamic surface activity of the dipalmitoyl phosphatidyl choline (DPPC) [6,7].…”