Thermodynamics of Micelle Formation as a Function of Temperature: A High Sensitivity Titration Calorimetry Study

1995 ◽  
Vol 99 (30) ◽  
pp. 11742-11751 ◽  
Author(s):  
Stefan Paula ◽  
Willy Sues ◽  
Juergen Tuchtenhagen ◽  
Alfred Blume
Keyword(s):  
Micelle Formation ◽  
High Sensitivity ◽  
Titration Calorimetry ◽  
Thermodynamics Of Micelle Formation

Thermodynamics of Micelle Formation of the Counterion Coupled Gemini Surfactant Bis(4-(2-dodecyl)benzenesulfonate)-Jeffamine Salt and Its Dynamic Adsorption on Sandstone

2008 ◽  
Vol 112 (48) ◽  
pp. 15320-15326 ◽  
Author(s):  
Annamária B. Páhi ◽  
Zoltán Király ◽  
Ágnes Mastalir ◽  
József Dudás ◽  
Sándor Puskás ◽  
...  
Keyword(s):  
Gemini Surfactant ◽  
Micelle Formation ◽  
Dynamic Adsorption ◽  
Thermodynamics Of Micelle Formation

Titration calorimetry of surfactant–drug interactions: Micelle formation and saturation studies

2012 ◽  
Vol 53 ◽  
pp. 36-41 ◽  
Author(s):  
Laura J. Waters ◽  
Talib Hussain ◽  
Gareth M.B. Parkes
Keyword(s):  
Drug Interactions ◽  
Micelle Formation ◽  
Titration Calorimetry

scholarly journals Evaluation of the stoichiometry and energetics of carbohydrate binding to Ricinus communis agglutinin: a calorimetric study

1998 ◽  
Vol 333 (3) ◽  
pp. 539-542 ◽  
Author(s):  
Shalini SHARMA ◽  
Satish BHARADWAJ ◽  
Avadhesha SUROLIA ◽  
Sunil Kumar PODDER
Keyword(s):  
Ricinus Communis ◽  
Binding Constants ◽  
High Sensitivity ◽  
Titration Calorimetry ◽  
Water Molecules ◽  
Carbohydrate Binding ◽  
Calorimetric Study ◽  
Ricinus Communis Agglutinin ◽  
Preferential Binding ◽  
Site Binding

High-sensitivity isothermal titration calorimetry has been used to investigate the thermodynamics of binding of Ricinus communis agglutinin to galactose, lactose and their derivatives in the temperature range 280.5–298 K. The present study unequivocally establishes the carbohydrate-binding stoichiometry of the tetrameric agglutinin from castor bean as two, i.e. the (As–sB)2-type tetramer of the agglutinin has two equivalent sites that are non-interacting and independent. The site binding constants range from 2.2×103 M-1 at 282 K for galactose to 4.84×104 M-1 at 281 K for N-acetyl-lactosamine. The binding enthalpies range from -21.9 kJ·mol-1 at 293 K for 4-methylumbelliferyl-β-galactoside to -50.2 kJ·mol-1 at 292.9 K for thiodigalactoside. The observation of limited entropy–enthalpy compensation for binding of the sugars to the lectin indicates that reorganization of water molecules plays an important role in binding. As the slope of the compensation plot is greater than unity, the reactions are largely enthalpically driven. These studies show that the stronger binding of N-acetyl-lactosamine than lactose is due to a favourable interaction between the acetamido group of the reducing-end N-acetylglucosamine of the former and the corresponding loci in the agglutinin molecule. Preferential binding of methyl-β-galactoside over methyl-α-galactoside also indicates the apolar nature of the interaction with the methyl group of the former sugar.

THE THERMODYNAMICS OF MICELLE FORMATION IN ASSOCIATION COLLOIDS

1962 ◽  
Vol 66 (7) ◽  
pp. 1375-1376 ◽  
Author(s):  
Pasupati Mukerjee
Keyword(s):  
Micelle Formation ◽  
Association Colloids ◽  
Thermodynamics Of Micelle Formation
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