Adsorption of collagen, serum albumin, and fibronectin to glass and to each other

Meltzer, Hagar; Silberberg, A.

doi:10.1016/0021-9797(88)90123-3

Cited by 10 publications

(6 citation statements)

References 12 publications

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“…The pipets and chamber surfaces were incubated in an aqueous 0.2 g % solution of bovine serum albumin (BSA, fatty acid free, Sigma) for 15-30 min to prevent the lipidcoated bubbles from sticking to the glass. 29 The BSA solution was removed and replaced by PBS prior to the experiment.…”

Section: Methodsmentioning

confidence: 99%

“…The dual transducer system made possible the measurement of pressures ranging from the on order of 10 -1 −10 4 Pa (10 -6 −10 -1 atm). The pipets and chamber surfaces were incubated in an aqueous 0.2 g % solution of bovine serum albumin (BSA, fatty acid free, Sigma) for 15−30 min to prevent the lipid-coated bubbles from sticking to the glass . The BSA solution was removed and replaced by PBS prior to the experiment.…”

Section: Methodsmentioning

confidence: 99%

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Mechanical Properties and Microstructure of Polycrystalline Phospholipid Monolayer Shells: Novel Solid Microparticles

et al. 2003

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W This paper contains enhanced objects available on the Internet at http://pubs.acs.org/ journals/langd5.A polycrystalline phospholipid monolayer self-assembled at the surface of an air microbubble in aqueous solution represents a novel material structure: in essence, a solid shell of wax with micrometer-scale dimensions and a thickness of only a single molecule. Micropipet manipulation of these microparticles revealed the dependence of the mechanical properties of the lipid shells, specifically, yield shear and shear viscosity, on the composition, grain microstructure, and thermal processing of the material, in particular the cooling rate of the shells from the melt. Properties were measured as a function of the (1) lipid composition at a fixed cooling rate and (2) cooling rate at a fixed lipid composition. Epifluorescent microscopy and transmission electron microscopy revealed that the morphology of the 1,2-distearoyl-sn-glycero-3-phosphatidylcholine monolayer microstructure, which develops upon freezing from the melt, is dependent on the cooling rate through the lipid transition temperature Tm, with larger micrograins being formed at slower cooling rates. Mechanical properties of the lipid shell follow micrograin size, with the coarse grain structure exhibiting a higher resistance to shear deformation than the fine grain structure does, which is behavior consistent with that of more traditional bulk crystalline materials. IntroductionThe same principles of self-assembly that describe the formation and structure of a lipid monolayer on a flat trough of water also apply to the spontaneous organization of amphiphilic material at a curved gas-liquid interface such as that posed by the surface of an air microbubble in water. 1-3 It is well-known that at sufficient concentrations the surface contaminants on a "dirty" bubble in water can effectively immobilize the air-water interface and cause the bubble to behave as a rigid particle. A relatively recent addition to the family of experimental techniques for studying monolayer properties known as axisymmetric drop shape analysis (ADSA) was employed by Kwok and co-workers as a film balance, albeit on a curved droplet surface, to obtain surface pressure-surface area (Π-A) isotherms for monolayer films of 1-octadecanol. 4,5 ADSA experiments have demonstrated the equivalence of curved monolayers and flat monolayers with respect to surface phase states and transitions. Until recently, however, the direct measurement of the mechanical properties of monolayers spread at micrometer-scale curved interfaces has eluded investigators; furthermore, extant work on monolayers, whether on flat or curved interfaces, has been mostly confined to the liquid-expanded or liquid-condensed-expanded coexistence regimes of their phase diagrams. The current study presents the first mechanical property measurements made for solid lipid monolayer shells of well-defined composition and micrograin structure formed on the surfaces of gas microbubbles, thus essentially comprising gas microparticles s...

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Mechanical Properties and Microstructure of Polycrystalline Phospholipid Monolayer Shells: Novel Solid Microparticles

et al. 2003

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“…Before the experiment, the chamber and the inner and outer surfaces of the pipettes were incubated in 0.2 g % aqueous solution of BSA for 15-30 min to eliminate the sticking of vesicles to the glass (37). The BSA solution was then flushed out of the chamber several times with BSA-free PBS.…”

Section: Micropipette Manipulationmentioning

confidence: 99%

Effects of Amyloid β-Peptides on the Lysis Tension of Lipid Bilayer Vesicles Containing Oxysterols

Kim

Frangos

2008

Biophysical Journal

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Amyloid beta-peptides (Abeta) applied directly from solution to model lipid membranes produced dramatic changes in the material properties of the bilayer when certain oxysterols were present in the bilayer. These effects were dependent on both lipid and peptide composition, and occurred at peptide concentrations as low as 100 nM. Using micropipette manipulation of giant unilamellar vesicles, we directly measured the lysis tension of lipid bilayers of various compositions. The glycerophospholipid 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine (SOPC) constituted the main lipid component at 70 mol %. The remaining 30 mol % was composed of the following pure or mixed sterols: cholesterol (CHOL), 7-ketocholesterol (KETO), or 7beta-hydroxycholesterol (OHCHOL). SOPC/CHOL bilayers did not exhibit significant changes in mechanical properties after exposure to either Abeta(1-42) or Abeta(1-40). Partial substitution of CHOL with KETO (5 mol %), however, caused a drastic reduction of the lysis tension after exposure to Abeta(1-42) but not to Abeta(1-40). Partial substitution of CHOL with OHCHOL (5 mol %) caused a drastic reduction of the lysis tension after exposure to Abeta(1-40) and to Abeta(1-42). We attribute these effects to the reduction in intermolecular cohesive interactions caused by the presence of the second dipole of oxysterols, which reduces the energetic barrier for Abeta insertion into the bilayer.

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“…As the diameter of each arm of the fibronectin molecule is about 2 nm, such a configuration could lead to a thin film not detectable by the XPS technique. According to Addadi et al, 13 the interaction of fibronectin with the substrate surface occurs through certain domains of the molecule, and it is conceivable that adsorbed fibronectin molecules adopt a spread conformation due to interdomain modifications. Independent of the structure of the adsorbed fibronectin layer, the small concentrations of both FN solutions, compared with the saturation value of 0.1 mg/mL reported for hydrophilic silica, 11 suggest that the substrate surfaces are far from being completely covered by the protein.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, fibronectin is known to contain calcium-sensitive heparin binding sites, which should interfere with the biomineralization of the titanium substrates. Although several studies of fibronectin adsorption onto solid substrates have been pub-lished, 9,[11][12][13][14] much work still has to be done in order to fully understand the interactions between this protein and biomaterial surfaces, in particular the role played by fibronectin in the process of the biomineralization of titanium implants immersed in acellular biological model fluids.…”

Section: Introductionmentioning

confidence: 99%

Calcium phosphate deposition on titanium surfaces in the presence of fibronectin

Serro¹,

Fernandes²,

Saramago³

2000

J. Biomed. Mater. Res.

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Titanium implants are known to nucleate spontaneously a calcium phosphate (apatite-like) layer when in contact with biological model fluids. The presence of proteins either in solution or pre-adsorbed on the titanium surface may influence the process of calcium phosphate deposition. The role of fibronectin, a protein known to promote cell adhesion in spite of its low concentration in biological fluids, was dissolved in Hanks' balanced salt solution (HBSS) and investigated. Several techniques of surface analysis, namely wettability, XPS, and SEM studies, were applied. The concentration of fibronectin in the HBSS solution was an important parameter in the process of calcium phosphate deposition. Concentrations as low as 0.01 mg/mL did not significantly affect the ionic precipitation; however, if the protein concentration was increased to 0.05 mg/mL, a value still far below the concentration in blood (0.2 mg/mL), the formation of a calcium phosphate layer was strongly inhibited. The influence of fibronectin pre-adsorbed on titanium surface also was investigated. It was found, as in the first case, that the extent of ionic precipitation that occurred during the immersion in HBSS depended on the protein concentration in the NaCl solution used to pre-immerse the titanium sample.

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Adsorption of collagen, serum albumin, and fibronectin to glass and to each other

Cited by 10 publications

References 12 publications

Mechanical Properties and Microstructure of Polycrystalline Phospholipid Monolayer Shells: Novel Solid Microparticles

Mechanical Properties and Microstructure of Polycrystalline Phospholipid Monolayer Shells: Novel Solid Microparticles

Effects of Amyloid β-Peptides on the Lysis Tension of Lipid Bilayer Vesicles Containing Oxysterols

Calcium phosphate deposition on titanium surfaces in the presence of fibronectin

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