Adsorption and surface tension of fibrinogen at the air/water interface

Hernández, Erika M.; Franses, Elias I.

doi:10.1016/s0927-7757(02)00403-x

Cited by 31 publications

(16 citation statements)

References 20 publications

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“…This interface was much more mobile than the more homogeneous layers formed by HF-OG at higher concentrations. The expected surface tension for this HF solution at the time of this image is ∼60 mN/m . This image implies that HF aggregates at the interface and results in a series of islands of aggregated HF surrounded by areas of nonaggregated HF.…”

Section: Resultsmentioning

confidence: 80%

Imaging Macromolecular Interactions at an Interface

et al. 2010

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Important physiological, pathological, and technological processes occur at continuous and dispersed phase interfaces. Understanding these processes is limited by inability to quantitate molecular events occurring at the interface. To provide a model-independent measurement of protein concentration and mobility at the interface, we employed confocal laser scanning microscopy (CLSM). Fluorescently labeled albumin and fibrinogen were studied singly, pairwise, and with a surfactant, Pluronic F-127, in aqueous droplets. CLSM enables measurement of molecular behaviors manifest as surface inhomogeneity and of biophysical quantities including partitioning between the bulk and the gas-liquid (GL) interface. We conclude that albumin and fibrinogen behave substantially differently at the GL interface, that adsorption from multi-species solutions is fundamentally different than adsorption from solutions of single species, and surfactants can inhibit proteins from occupying the interface.

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Section: Resultsmentioning

confidence: 80%

Imaging Macromolecular Interactions at an Interface

et al. 2010

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“…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%

“…Informed and inspired by these observations, we present a physico-chemical study of fibrinogen, which is believed to inhibit LS function more severely than other blood proteins [18,20], characterizing its effect on a model phospholipid monolayer under idealized, laboratory conditions. Fibrinogen adsorbs at an aqueous -air interface, forming a monolayer of molecules which become increasingly aligned with increasing surface density [24][25][26][27], and therefore may compete with LS to adsorb in the alveoli, potentially promoting inactivation. Thus, it is important to understand fibrinogen's effect on surface tension, and how it alters the structural and rheological properties of phospholipid monolayers.…”

Section: Introductionmentioning

confidence: 99%

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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“…Similarly, fibrinogen was shown to adsorb at the air/water interface. 26,27 For example, Ariola et al 27 investigated the interfacial adsorption of fibrinogen with interfacial rheology. However, those solutions were too dilute (< 25 × 10 -11 mg/mL) to have any significance for DOD inkjet printing and the influence of interfacial adsorption on the bulk rheology measurements was not reported.…”

Section: Introductionmentioning

confidence: 99%

Rheological Investigation of Collagen, Fibrinogen, and Thrombin Solutions for Drop-on-Demand 3D Bioprinting

Gudapati¹,

Parisi²,

Colby³

et al. 2020

Preprint

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<p>Collagen, fibrinogen, and thrombin proteins in aqueous buffer solutions are widely used as precursors of natural biopolymers for three-dimensional (3D) bioprinting applications. The proteins are sourced from animals and their quality may vary from batch to batch, inducing differences in the rheological properties of such solutions. In this work, we investigate the rheological response of collagen, fibrinogen, and thrombin protein solutions in bulk and at the solution/air interface. Interfacial rheological measurements show that fibrous collagen, fibrinogen and globular thrombin proteins adsorb and aggregate at the solution/air interface, forming a viscoelastic solid film at the interface. The viscoelastic film corrupts the bulk rheological measurements in rotational rheometers by contributing to an apparent yield stress, which increases the apparent bulk viscosity up to shear rates as high as 1000 s<sup>-1</sup>. The addition of a non-ionic surfactant, such as polysorbate 80 (PS80) in small amounts between 0.001 and 0.1 v/v%, prevents the formation of the interfacial layer, allowing the estimation of true bulk viscosity and viscoelastic properties of the solutions. The estimation of viscosity not only helps in identifying those protein solutions that are potentially printable with drop-on-demand (DOD) inkjet printing but also detects inconsistencies in flow behavior among the batches.</p>

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Adsorption and surface tension of fibrinogen at the air/water interface

Cited by 31 publications

References 20 publications

Imaging Macromolecular Interactions at an Interface

Imaging Macromolecular Interactions at an Interface

Evolution and mechanics of mixed phospholipid fibrinogen monolayers

Rheological Investigation of Collagen, Fibrinogen, and Thrombin Solutions for Drop-on-Demand 3D Bioprinting

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