Two novel C16:0
sulfur-linked
phosphonolipids (S-lipid and SO(2)-lipid) and two
ether-linked
phosphonolipids (C16:0
DEPN-8 and C16:1 UnDEPN-8) were studied for surface behavior alone and in mixtures with purified
bovine lung surfactant proteins (SP)-B and/or SP-C. Synthetic C16:0
phosphonolipids all had improved adsorption and film respreading compared to
dipalmitoyl phosphatidylcholine, and SO(2)-lipid and
DEPN-8 reached maximum surface pressures of 72mN/m (minimum surface tensions of <1mN/m) in compressed films on the Wilhelmy balance (23 degrees C). Dispersions of
DEPN-8 (0.5mg/ml) and SO(2)-lipid (2.5mg/ml) also reached minimum surface tensions of <1mN/m on a pulsating bubble surfactometer (37 degrees C, 20cycles/min, 50% area compression). Synthetic lung
surfactants containing
DEPN-8 or SO(2)-lipid+0.75% SP-B+0.75% SP-C had dynamic surface activity on the bubble equal to that of calf lung
surfactant extract (CLSE).
Surfactants containing
DEPN-8 or SO(2)-lipid plus 1.5% SP-B also had very high surface activity, but less than when both
apoproteins were present together. Adding 10wt.% of UnDEPN-8 to synthetic lung
surfactants did not improve dynamic surface activity.
Surfactants containing
DEPN-8 or SO(2)-lipid plus 0.75% SP-B/0.75% SP-C were chemically and biophysically resistant to
phospholipase A(2) (PLA(2)), while CLSE was severely inhibited by PLA(2). The high activity and inhibition resistance of synthetic
surfactants containing
DEPN-8 or SO(2)-lipid plus SP-B/SP-C are promising for future applications in treating
surfactant dysfunction in inflammatory
lung injury.