Rheologic hysteresis curve shape specificity of mixed lipid films

Lusted, Dean

doi:10.1016/0005-2736(73)90094-1

Cited by 9 publications

(5 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, it cannot be ruled out that rearrangements within the monolayer may also have an effect. Sphingomyelins have previously been reported to form metastable monolayers. , In agreement with the present study, it was shown, from constant area−Π measurements, that monolayers of sphingomyelins were stable up to 20 mN/m . To give further information concerning the instability of the sphingomyelin monolayer, additional experiments were performed.…”

Section: Resultssupporting

confidence: 91%

Bovine Milk Sphingomyelin at the Air/Water Interface and Its Interaction with Xanthine Oxidase

Kristensen¹,

Nylander²,

Rasmussen³

et al. 1996

Langmuir

View full text Add to dashboard Cite

The monolayer properties of two different sphingomyelin samples from bovine milk (one pure with respect to sphingomyelin (>99%) and one sphingolipid fraction containing 68% sphingomyelin) at the air/water interface and the interaction between the lipid monolayer and xanthine oxidase (XO) from the milk fat globule membrane were investigated by the film balance technique. For comparison, similar measurements were performed on distearoylphosphatidylcholine (DSPC) monolayers. Bovine milk sphingomyelin formed monolayers comparable with those of other natural sphingomyelins. A liquid-condensed phase transition at 20−22 mN/m reflected the high amount of long saturated fatty acids, as in the case for monolayers of egg sphingomyelin. Monolayers of bovine milk sphingomyelin were metastable, as opposed to those of DSPC. The observed decrease in surface area with time at constant pressure indicated that dissolution/expulsion into the subphase took place. A pure sphingomyelin monolayer was significantly more stable at a surface pressure of 10 mN/m than at 20 mN/m. The discontinuity in the surface area change versus time and the low solubility of the lipid show that the instability cannot be explained by simple desorption of lipid monomers. The presence of XO in the subphase increased the maximal surface pressure at an area per molecule of sphingomyelin of 30 Å2 (maximal compression) by 15 mN/m for the sphingolipid sample and 20 mN/m for pure sphingomyelin, indicating a stabilization of sphingomyelin monolayers in the presence of XO at high surface pressure. This effect was not observed for DSPC monolayers, which suggests a specific interaction between sphingomyelin and XO.

show abstract

Section: Resultssupporting

confidence: 91%

Bovine Milk Sphingomyelin at the Air/Water Interface and Its Interaction with Xanthine Oxidase

Kristensen¹,

Nylander²,

Rasmussen³

et al. 1996

Langmuir

View full text Add to dashboard Cite

show abstract

“…3a ). The hysteresis shown in the isotherms is common for membrane lipids and surface‐active proteins [11,14,15]; in the case of glycogenin it amounts to a rather high compression free energy gap of 27.3 kcal/mol. This indicates that the protein intermolecular organization at the surface is capable, over the long range, of conserving information of the molecular state acquired initially under spreading, and after it has reached the compressed packing state.…”

Section: Resultsmentioning

confidence: 99%

The amphiphilic character of glycogenin

Carrizo¹,

Miozzo²,

Maggio³

et al. 2001

FEBS Letters

View full text Add to dashboard Cite

This study describes for the first time the amphiphilicity of the protein moiety of proteoglycogen. Glycogenin but not proteoglycogen associates to phospholipid vesicles and forms by itself stable Gibbs and Langmuir monolayers at the air^buffer interface. The adsorption free energy (3 36.7 kcal/mol) and the glycogenin collapse pressure (47 mN/m) are indicative of its high surface activity which can thermodynamically drive and retain the protein at the membrane interface to a maximum equilibrium adsorption surface pressure of 21 mN/m. The marked surface activity of glycogenin is further enhanced by its thermodynamically favorable penetration into zwitterionic and anionic phospholipids with a high cut-off surface pressure point above 30 mN/m. The strong association to phospholipid vesicles and the marked surface activity of glycogenin correspond to a high amphiphilic character which supports its spontaneous association to membrane interfaces, in which the de novo biosynthesis of glycogen was proposed to initiate. ß 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

show abstract

“…The hysteresis, corresponding to a free energy gap of 16 kcal/mol between compression and decompression calculated using isotherms similar to those shown in Fig. 3A, is larger than that of c-Fos and other membrane proteins [13,[26][27][28]. This can be due to the fact that c-Jun has a significantly more expanded character than c-Fos at the interface.…”

Section: C-jun Is Amphitropic and Interacts With Phospholipidsmentioning

confidence: 84%