Monolayer and Brewster angle microscopy study of human serum albumin—Dipalmitoyl phosphatidyl choline mixtures at the air–water interface

Toimil, Paula; Prieto, Gerardo; Miñones, J.; Trillo, José Miñones; Sarmiento, Félix

doi:10.1016/j.colsurfb.2011.11.022

Cited by 33 publications

(13 citation statements)

References 57 publications

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“…Finally, comparing these results with the obtained for DPPC/ HSA mixed monolayers [49], can be conclude that the presence of a fluorine atom in the tail of the phospholipids does not hardly affects the surface behavior of the lipid-protein system, so the obtained results have showed that the mono fluorinated phospholipids may be useful to improve the design of liposomes used as drug delivery since they are less toxic than the poly fluorinated compounds and more stable than the hydrogenated one.…”

Section: Discussionmentioning

confidence: 68%

Interaction of human serum albumin with monofluorinated phospholipid monolayers

Toimil

Prieto

Miñones

et al. 2012

Journal of Colloid and Interface Science

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Section: Discussionmentioning

confidence: 68%

Interaction of human serum albumin with monofluorinated phospholipid monolayers

Toimil

Prieto

Miñones

et al. 2012

Journal of Colloid and Interface Science

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“…That is to say, aggregation occurs both below and above the BSA isoelectric point (≈4.8), although interaction is stronger at higher subphase pH [80]. Only one layer of BSA forms below the lipid monolayer with their long axis parallel to the lipid monolayer.…”

Section: Accepted Manuscriptmentioning

confidence: 94%

“…Human Serum Albumin (HAS) and Bovine Serum Albumin (BSA) have been reported as good examples to study adsorption at lipid Langmuir monolayers [80,81]. With Brewster angle microscopy one may estimate the thickness of DPPC monolayers upon HAS incorporation [80].…”

Section: Accepted Manuscriptmentioning

confidence: 99%

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Interactions of bioactive molecules & nanomaterials with Langmuir monolayers as cell membrane models

et al. 2015

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“…From the reported literatures we can know that the presence of BSA in the subphase definitely affected the compressional elasticity of the films at the air-water [7]. The compressibility coefficient (C −1 S ) is a useful parameter to quantify the compression elasticity of the films and phase transition behaviors [36,37], which is defined as…”

Section: B Compressibility Analysismentioning

confidence: 99%

Dynamic Behaviors and Morphology Change of Anionic Phospholipid DPPG Monolayer Caused by Bovine Serum Albumin at Air-Water Interface

Xu¹,

Hao²,

Zhang³

et al. 2017

Chinese Journal of Chemical Physics

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The interaction between bovine serum albumin (BSA) and the anionic 1.2-dipalmitoyl-snglycero-3-(phospho-rac-(1-glycerol)) (sodium salt) (DPPG) phospholipid at different subphase pH values was investigated at air-water interface through surface pressure measurements and atomic force microscopy (AFM) observation. By analyzing surface pressure-mean molecular area (π-A) isotherms, the limiting molecular area in the closed packing state-the concentration of BSA (A lim -[BSA]) curves, the compressibility coefficient-surface pressure (C −1 S -π) curves and the difference value of mean molecular area-the concentration of BSA (∆A-[BSA]) curves, we obtained that the mean molecular area of DPPG monolayer became much larger when the concentration of BSA in the subphase increased at pH=3 and 5. But the isotherms had no significant change at different amount of BSA at pH=10. In addition, the amount of BSA molecules adsorbed onto the lipid monolayer reached a threshold value when [BSA]>5×10 −8 mol/L for all pHs. From the surface pressure-time (π-t) data, we obtained that desorption and adsorption processes occurred at pH=3, however, there was only desorption process occurring at pH=5 and 10. These results showed that the interaction mechanism between DPPG and BSA molecules was affected by the pH of subphase. BSA molecules were adsorbed onto the DPPG monolayers mainly through the hydrophobic interaction at pH=3 and 5, and the strength of hydrophobic interaction at pH=3 was stronger than the case of pH=5. At pH=10, a weaker hydrophobic interaction and a stronger electrostatic repulsion existed between DPPG and BSA molecules. AFM images revealed that the pH of subphase and [BSA] could affect the morphology features of the monolayers, which was consistent with these curves. The study provides an important experimental basis and theoretical support to understand the interaction between lipid and BSA at the air-water interface.

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Monolayer and Brewster angle microscopy study of human serum albumin—Dipalmitoyl phosphatidyl choline mixtures at the air–water interface

Cited by 33 publications

References 57 publications

Interaction of human serum albumin with monofluorinated phospholipid monolayers

Interaction of human serum albumin with monofluorinated phospholipid monolayers

Interactions of bioactive molecules & nanomaterials with Langmuir monolayers as cell membrane models

Dynamic Behaviors and Morphology Change of Anionic Phospholipid DPPG Monolayer Caused by Bovine Serum Albumin at Air-Water Interface

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