Dynamic Interfacial Properties of Surface-excess Films of Phospholipids and Phosphonolipid Analogs

Liu, Huicai; Turcotte, Joseph G.; Notter, Robert H.

doi:10.1006/jcis.1994.1374

Cited by 20 publications

(18 citation statements)

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“…The excellent surface tension lowering ability of DPPC, aided to some degree by other rigid saturated PCs in lung surfactant (6), is directly complemented by the ability of fluid, unsaturated PCs to facilitate adsorption (11,39,43) and improve film respreading (22-24, 38). These latter behaviors may also be contributed to by additional secondary phospholipids having non-PC headgroups (11,44), but the secondary PCs should be particularly important both because of their greater relative concentration and their potential for specific interactions and miscibility with DPPC because of their identical headgroup.…”

Section: Discussionmentioning

confidence: 97%

Primary Importance of Zwitterionic Over Anionic Phospholipids in the Surface-active Function of Calf Lung Surfactant Extract

Wang

Gurel

Weinbach

et al. 1997

Am J Respir Crit Care Med

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The relative contributions of zwitterionic and anionic phospholipids to the surface-active function of calf lung surfactant extract (CLSE) were assessed by measurements of surface properties in vitro and pressure-volume (P-V) mechanics in excised rat lungs in situ. Surface activity and mechanical effects were compared for chromatographically purified CLSE subfractions containing the complete mix of phospholipids (PPL) or modified phospholipids depleted in anionic components (mPPL), alone or combined with 1.3% (by weight) of hydrophobic surfactant proteins (SP-B and SP-C). Surface pressure-time (pi-t) adsorption isotherms at 37 degrees C were very similar for dispersions of PPL and mPPL in a Teflon dish with a stirred subphase to minimize diffusion resistance. Combination of either PPL or mPPL with hydrophobic SP substantially improved adsorption, but mixtures of PPL:SP and mPPL:SP had only small differences in pi-t isotherms and reached the same final equilibrium pi of approximately 47 mN/m achieved by CLSE. Surface pressure-area (pi-A) isotherms and maximum surface pressures were also very similar for spread films of PPL versus mPPL and PPL:SP versus mPPL:SP on the Wilhelmy balance (23 degrees C and 37 degrees C). Respreading based on pi-A isotherm area calculations was slightly better in surface-excess films of PPL versus mPPL and PPL:SP versus mPPL:SP, but differences were minor and were smaller at 37 degrees C than at 23 degrees C. Overall dynamic surface activity in oscillating bubble studies was not significantly different for PPL versus mPPL or for PPL:SP versus mPPL:SP, and the latter two mixtures both reached minimum surface tensions< 1 mN/m (37 degrees C, 20 cycles/min, 0.5 mM phospholipid). Dispersions of PPL:SP, mPPL:SP, and CLSE were also not significantly different in improving P-V mechanics almost to normal when instilled in lavaged, excised rat lungs at 37 degrees C (30 mg/2.5 ml saline). These data suggest that zwitterionic phospholipids have a major role over anionic phospholipids in interacting with hydrophobic SP in the adsorption, dynamic surface tension lowering, film respreading, and pulmonary mechanical activity of the hydrophobic components of calf lung surfactant in CLSE.

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Section: Discussionmentioning

confidence: 97%

Primary Importance of Zwitterionic Over Anionic Phospholipids in the Surface-active Function of Calf Lung Surfactant Extract

Wang

Gurel

Weinbach

et al. 1997

Am J Respir Crit Care Med

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“…DEPN-8 also has ether, rather than ester, linkages between the fatty chains and the glycerol backbone, plus a methylene for oxygen substitution in the head group so that it is a phosphonolipid rather than a phospholipid (30,51,52). Ether linkages in DEPN-8 increase chain mobility and facilitate film respreading during cycling (31,32,52). Films of DEPN-8 ϩ 1.5% SP-B/C in the present study had very impressive respreading, which exceeded that degrading extracted bovine lung surfactant (CLSE) and DEPN-8 ϩ 1.5% bovine SP of CLSE, based on collapse plateau ratios for cycle 7/cycle 1 (but not cycle 2/cycle 1) ( Table 1).…”

Section: Discussionmentioning

confidence: 99%

Surface activity of a synthetic lung surfactant containing a phospholipase-resistant phosphonolipid analog of dipalmitoyl phosphatidylcholine

Wang¹,

Schwan²,

Lairson³

et al. 2003

American Journal of Physiology-Lung Cellular and Molecular Phys

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Surface activity of a synthetic lung surfactant containing a phospholipase-resistant phosphonolipid analog of dipalmitoyl phosphatidylcholine. Am J Physiol Lung Cell Mol Physiol 285: L550-L559, 2003; 10.1152/ajplung.00346.2002.-Surface activity and sensitivity to inhibition from phospholipase A2 (PLA2), lysophosphatidylcholine (LPC), and serum albumin were studied for a synthetic C16:0 diether phosphonolipid (DEPN-8) combined with 1.5% by weight of mixed hydrophobic surfactant proteins (SP)-B/C purified from calf lung surfactant extract (CLSE). Pure DEPN-8 had better adsorption and film respreading than the major lung surfactant phospholipid dipalmitoyl phosphatidylcholine and reached minimum surface tensions Ͻ1 mN/m under dynamic compression on the Wilhelmy balance and on a pulsating bubble surfactometer (37°C, 20 cycles/min, 50% area compression). DEPN-8 ϩ 1.5% SP-B/C exhibited even greater adsorption and had overall dynamic surface tension lowering equal to CLSE on the bubble. In addition, films of DEPN-8 ϩ 1.5% SP-B/C on the Wilhelmy balance had better respreading than CLSE after seven (but not two) cycles of compression-expansion at 23°C. DEPN-8 is structurally resistant to degradation by PLA2, and DEPN-8 ϩ 1.5% SP-B/C maintained high adsorption and dynamic surface activity in the presence of this enzyme. Incubation of CLSE with PLA2 led to chemical degradation, generation of LPC, and reduced surface activity. DEPN-8 ϩ 1.5% SP-B/C was also more resistant than CLSE to direct biophysical inhibition by LPC, and the two were similar in their sensitivity to biophysical inhibition by serum albumin. These findings indicate that synthetic surfactants containing DEPN-8 combined with surfactant proteins or related synthetic peptides have potential utility for treating surfactant dysfunction in inflammatory lung injury. exogenous surfactants; phospholipid analogs; phospholipase A2; phospholipase resistance; inhibition resistance; diether phosphonolipid; surfactant proteins ENDOGENOUS LUNG SURFACTANT contains functionally important lipids and apoproteins (37), and its activity is compromised when these essential components are chemically degraded or altered. One important cause of such effects is through the action of phospholipases or proteases during inflammatory lung injury. Lytic enzymes of this kind can degrade and inactivate not only endogenous surfactant, but also exogenous lung surfactants used in treating clinical acute lung injury and the acute respiratory distress syndrome (ARDS). All current exogenous surfactant drugs contain substantial contents of glycerophospholipids including 1,2-dipalmitoyl-sn-3-phosphatidylcholine (DPPC), the most prevalent component of endogenous lung surfactant. Phospholipase-induced degradation of glycerophospholipids not only reduces the concentration of active surfactant but also generates byproducts like lysophosphatidylcholine (LPC) and fluid free fatty acids that can further decrease surface activity through biophysical interactions (21, 37, 59). Synthetic exogenous surfactan...

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“…The predominant surface tension lowering lipid component in native lung surfactant is 29, dipalmitoyl phosphatidylcholine (DPPC). Diether phosphonolipid analog 28 is a very promising substitute for DPPC in synthetic exogenous lung surfactant preparations [54,55,[56][57][58][59][60][61]. Not only can 28 match the ability of DPPC to reach extremely low surface tensions in compressed surface films, but it also exhibits superior adsorption and film spreading behaviors while incorporating a resistance to degradation by Downloaded by [The University of Manchester Library] at 02: 25 12 October 2014 lytic phospholipase enzymes that can be present in the pulmonary interstitium and alveoli during inflammatory injury [54,[55][56][57][58][59][60][61].…”

Section: Thioether Lipidsmentioning

confidence: 99%

Synthesis of sulfur-containing glycerophospholipids

Davy

Wang

Notter

et al. 2007

Journal of Sulfur Chemistry

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Dynamic Interfacial Properties of Surface-excess Films of Phospholipids and Phosphonolipid Analogs

Cited by 20 publications

References 0 publications

Primary Importance of Zwitterionic Over Anionic Phospholipids in the Surface-active Function of Calf Lung Surfactant Extract

Primary Importance of Zwitterionic Over Anionic Phospholipids in the Surface-active Function of Calf Lung Surfactant Extract

Surface activity of a synthetic lung surfactant containing a phospholipase-resistant phosphonolipid analog of dipalmitoyl phosphatidylcholine

Synthesis of sulfur-containing glycerophospholipids

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