Mixed Monolayer and Micelle Formation of Cationic and Zwitterionic Surfactant of Identical Hydrocarbon Tail in an Aqueous Medium: Interfacial Tension, Fluorescence Probe, Dynamic Light Scattering, and Viscosity Studies

2008 ◽  
Vol 29 (3) ◽  
pp. 327-334 ◽  
Author(s):  
Pankaj Sehgal ◽  
Hidekazu Doe ◽  
Reinhard Wimmer ◽  
Reiji Tanaka ◽  
Osamu Kosaka
Author(s):  
Natalia V. Mironenko ◽  
Irina V. Shkutina ◽  
Vladimir F. Selemenev

The regularities of changes in structural characteristics during the formation of associates in micellar aqueous solutions of triterpene saponins Quillaja Saponin and Sapindus Mukorossi are considered. The dependence of surface tension and adsorption on the concentration of an aqueous saponin solution is analyzed, and the values of surface activity and parameters of the adsorption layer are calculated. The average values of diffusion coefficients for spherical and cylindrical micelles are determined based on the measurement of the solution viscosity. The effect of the electrolyte solution on the surface tension and viscosity of glycoside solutions is studied: when the electrolyte is introduced into the saponin solution, the surface tension decreases, which leads to a shift in the critical concentration of micelle formation towards lower concentrations. The introduction of potassium chloride electrolyte reduces the degree of ionization and, as a result of suppressing the electroviscosity effect, leads to a decrease in the viscosity of the solution. The dynamic light scattering method is used to determine the size of glycoside aggregates. It is established that there are aggregates of several sizes in an aqueous solution of saponin. The size and shape of aggregates were calculated using the concepts of micelle packing parameters. In the region of very low concentrations of glycoside solutions, when approaching the critical concentration of micelle formation in the solution, there are spherical micelles. A further increase in the saponin concentration in the solution leads to a decrease in the content of structures with a hydrodynamic radius of 50-80 nm and the appearance of larger agglomerates with sizes greater than 100 nm. It was found that micelles acquire a less hydrated and more densely packed cylindrical shape in the concentration range of 1.7-2.6 mmol/dm3. Compaction of associates leads to an increase in the content of particles with a hydrodynamic radius of 150-250 nm and larger ones, and their presence predicts the appearance of larger agglomerates. Analyzing the data obtained using the dynamic light scattering method, it can be concluded that aggregates of several sizes co-exist in the volume of aqueous saponin solutions at certain concentrations.


Langmuir ◽  
1994 ◽  
Vol 10 (12) ◽  
pp. 4434-4439 ◽  
Author(s):  
V. J. Nagpal ◽  
R. M. Davis ◽  
Q. Liu ◽  
J. Facinelli ◽  
J. S. Riffle

Author(s):  
Arne Meyer ◽  
Karsten Dierks ◽  
Rana Hussein ◽  
Karl Brillet ◽  
Hevila Brognaro ◽  
...  

Detergents are widely used for the isolation and solubilization of membrane proteins to support crystallization and structure determination. Detergents are amphiphilic molecules that form micelles once the characteristic critical micelle concentration (CMC) is achieved and can solubilize membrane proteins by the formation of micelles around them. The results are presented of a study of micelle formation observed byin situdynamic light-scattering (DLS) analyses performed on selected detergent solutions using a newly designed advanced hardware device. DLS was initially appliedin situto detergent samples with a total volume of approximately 2 µl. When measured with DLS, pure detergents show a monodisperse radial distribution in water at concentrations exceeding the CMC. A series of all-transn-alkyl-β-D-maltopyranosides, fromn-hexyl ton-tetradecyl, were used in the investigations. The results obtained verify that the application of DLSin situis capable of distinguishing differences in the hydrodynamic radii of micelles formed by detergents differing in length by only a single CH2group in their aliphatic tails. Subsequently, DLS was applied to investigate the distribution of hydrodynamic radii of membrane proteins and selected water-insoluble proteins in presence of detergent micelles. The results confirm that stable protein–detergent complexes were prepared for (i) bacteriorhodopsin and (ii) FetA in complex with a ligand as examples of transmembrane proteins. A fusion of maltose-binding protein and theDuck hepatitis B virusX protein was added to this investigation as an example of a non-membrane-associated protein with low water solubility. The increased solubility of this protein in the presence of detergent could be monitored, as well as the progress of proteolytic cleavage to separate the fusion partners. This study demonstrates the potential ofin situDLS to optimize solutions of protein–detergent complexes for crystallization applications.


1978 ◽  
Vol 39 (9) ◽  
pp. 955-960 ◽  
Author(s):  
E. Geissler ◽  
A.M. Hecht

2014 ◽  
Vol 73 (11) ◽  
pp. 977-983
Author(s):  
A. P. Fedoryako ◽  
A. I. Kocherzhin ◽  
M. P. Kukhtin ◽  
E. I. Chernyakov

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