Displacement of Fibrinogen from the Air/Aqueous Interface by Dilauroylphosphatidylcholine Lipid

Phang, Tze-Lee; McClellan, Scott J; Franses, Elias I.

doi:10.1021/la0504412

Cited by 19 publications

(15 citation statements)

References 53 publications

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“…One conclusion to draw is that DPPC is not effective at removing fibrinogen that has already adsorbed to aqueousair interfaces, even when fibrinogen is so dilute that it has no measurable effect on P or interfacial rheology. This draws an intriguing contrast with previous research showing that dilauroylphosphatidylcholine (DLPC), a short-chain phospholipid which is partly soluble in water, can expel pre-adsorbed fibrinogen when adsorbing into fibrinogen monolayers from aqueous solution [39].…”

Section: Mixing Protocol I: Dipalmitoylphosphatidylcholine Added To Fcontrasting

confidence: 71%

“…While fibrinogen is known to adsorb at the aqueous -air interface [24][25][26]38,39], little attention has been paid to its interfacial shear rheology, either in equilibrium or during adsorption. Using a macroscopic rheometer, Ariola et al [37] measured steady-state interfacial moduli as a function of bulk concentration, c. Below an onset concentration, there is no measurable interfacial rheology.…”

Section: Fibrinogen Adsorptionmentioning

confidence: 99%

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Evolution and mechanics of mixed phospholipid fibrinogen monolayers

Williams¹,

Squires²

2018

J. R. Soc. Interface.

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All mammals depend on lung surfactant (LS) to reduce surface tension at the alveolar interface and facilitate respiration. The inactivation of LS in acute respiratory distress syndrome (ARDS) is generally accompanied by elevated levels of fibrinogen and other blood plasma proteins in the alveolar space. Motivated by the mechanical role fibrinogen may play in LS inactivation, we measure the interfacial rheology of mixed monolayers of fibrinogen and dipalmitoylphosphatidylcholine (DPPC), the main constituent of LS, and compare these to the single species monolayers. We find DPPC to be ineffective at displacing preadsorbed fibrinogen, which gives the resulting mixed monolayer a strongly elastic shear response. By contrast, how effectively a pre-existing DPPC monolayer prevents fibrinogen adsorption depends upon its surface pressure. At low DPPC surface pressures, fibrinogen penetrates DPPC monolayers, imparting a mixed viscoelastic shear response. At higher initial DPPC surface pressures, this response becomes increasingly viscous-dominated, and the monolayer retains a more fluid, DPPC-like character. Fluorescence microscopy reveals that the mixed monolayers exhibit qualitatively different morphologies. Fibrinogen has a strong, albeit preparation-dependent, mechanical effect on phospholipid monolayers, which may contribute to LS inactivation and disorders such as ARDS.

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Section: Mixing Protocol I: Dipalmitoylphosphatidylcholine Added To Fcontrasting

confidence: 71%

Section: Fibrinogen Adsorptionmentioning

confidence: 99%

Evolution and mechanics of mixed phospholipid fibrinogen monolayers

Williams¹,

Squires²

2018

J. R. Soc. Interface.

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“…As previously described, the PEO groups create a steric barrier to the adsorption of proteins [59][60][61]. However, there are no results in the present literature similar to the those obtained with IPL [27,51,58]. Furthermore, similar results were obtained when IPL and fibrinogen were injected simultaneously to the PBS subphase, further supporting this model (Supplementary Data Figure S8).…”

Section: Interactions Of Ipl and Fibrinogen In The Competitive Systemsupporting

confidence: 82%

“…Though this does not conclusively prove that IPL removed all fibrinogen molecules from the interface, it is clear that the monolayer behaved in a manner similar to that observed when significant amounts of fibrinogen were not present at the interface. Previous studies performed with DLPC or DPPC vesicles did not show this promising result of the prevention of protein adsorption in the presence fibrinogen pre-adsorbed to the monolayer [51,57,21,58].…”

Section: Interactions Of Ipl and Fibrinogen In The Competitive Systemmentioning

confidence: 78%

Restoration of the interfacial properties of lung surfactant with a newly designed hydrocarbon/fluorocarbon lipid

Dilli

Unsal

Uslu

et al. 2014

Colloids and Surfaces B: Biointerfaces

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“…A further advantage of using 35 kDa PEG compared to smaller molecular weights is the increased range of the depletion attraction (2 R g ). Other serum proteins such as fibrinogen have also been shown to competitively adsorb with lung surfactant lipids; fibrinogen is larger than albumin with dimensions of 5 × 5 × 46 nm [210]. While the exact orientation of fibrinogen at the air-liquid interface is unknown, the higher molecular weight PEG can likely generate a depletion attraction with sufficient range and magnitude to enhance surfactant adsorption.…”

Section: Optimizing Polymer Volume Fraction and Polymer Molecular Weightmentioning

confidence: 99%

Overcoming rapid inactivation of lung surfactant: Analogies between competitive adsorption and colloid stability

Zasadzinski

Stenger

Shieh

et al. 2010

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Lung surfactant (LS) is a mixture of lipids and proteins that line the alveolar air-liquid interface, lowering the interfacial tension to levels that make breathing possible. In acute respiratory distress syndrome (ARDS), inactivation of LS is believed to play an important role in the development and severity of the disease. This review examines the competitive adsorption of LS and surface-active contaminants, such as serum proteins, present in the alveolar fluids of ARDS patients, and how this competitive adsorption can cause normal amounts of otherwise normal LS to be ineffective in lowering the interfacial tension. LS and serum proteins compete for the air-water interface when both are present in solution either in the alveolar fluids or in a Langmuir trough. Equilibrium favors LS as it has the lower equilibrium surface pressure, but the smaller proteins are kinetically favored over multi-micron LS bilayer aggregates by faster diffusion. If albumin reaches the interface, it creates an energy barrier to subsequent LS adsorption that slows or prevents the adsorption of the necessary amounts of LS required to lower surface tension. This process can be understood in terms of classic colloid stability theory in which an energy barrier to diffusion stabilizes colloidal suspensions against aggregation. This analogy provides qualitative and quantitative predictions regarding the origin of surfactant inactivation. An important corollary is that any additive that promotes colloid coagulation, such as increased electrolyte concentration, multivalent ions, hydrophilic non-adsorbing polymers such as PEG, dextran, etc. or polyelectrolytes such as chitosan, added to LS, also promotes LS adsorption in the presence of serum proteins and helps reverse surfactant inactivation. The theory provides quantitative tools to determine the optimal concentration of these additives and suggests that multiple additives may have a synergistic effect. A variety of physical and chemical techniques including isotherms, fluorescence microscopy, electron microscopy and X-ray diffraction show that LS adsorption is enhanced by this mechanism without substantially altering the structure or properties of the LS monolayer.

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Displacement of Fibrinogen from the Air/Aqueous Interface by Dilauroylphosphatidylcholine Lipid

Cited by 19 publications

References 53 publications

Evolution and mechanics of mixed phospholipid fibrinogen monolayers

Evolution and mechanics of mixed phospholipid fibrinogen monolayers

Restoration of the interfacial properties of lung surfactant with a newly designed hydrocarbon/fluorocarbon lipid

Overcoming rapid inactivation of lung surfactant: Analogies between competitive adsorption and colloid stability

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