Mixed Aggregates of Surface-Active Ionic Liquids and 14-2-14 Gemini Surfactants in an Aqueous Medium as Fluid Scaffolds for Enzymology of Cytochrome-c

The aggregation behavior of the surface-active ionic liquid (SAIL), 3-(2-(hexadecyloxy)-2-oxoethyl)-1-methyl-1H-imidazol-3-ium chloride, [C16Emim][Cl], and a gemini surfactant (GS) (14-2-14) in the whole mole fraction range has been investigated in an aqueous medium employing various techniques. Exp...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 39(2023), 33 vom: 22. Aug., Seite 11582-11595
1. Verfasser: Singh, Manpreet (VerfasserIn)
Weitere Verfasser: Kumar, Sugam, Aswal, Vinod Kumar, Kang, Tejwant Singh
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2023
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article
Beschreibung
Zusammenfassung:The aggregation behavior of the surface-active ionic liquid (SAIL), 3-(2-(hexadecyloxy)-2-oxoethyl)-1-methyl-1H-imidazol-3-ium chloride, [C16Emim][Cl], and a gemini surfactant (GS) (14-2-14) in the whole mole fraction range has been investigated in an aqueous medium employing various techniques. Experimentally obtained values of critical aggregation concentration (cac) are in good agreement with the theoretical cac values obtained using Clint's equation. Rubingh's model has been employed to evaluate the extent of synergistic interactions between two components, which has been found to be dependent upon the composition of a mixture of surfactants. The polarity index, hydrodynamic diameter (Dh), zeta potential (ζ-Pot.), and morphology of the aggregates have been found to be dependent upon the extent of hydrophobic as well as dipolar interactions and the degree of counterion binding governed by the content of the GS in mixed aggregates. Thermodynamic parameters evaluated employing isothermal titration calorimetry have revealed the aggregation as an entropy-driven process. Density functional theory calculations provide a detailed account of the SAIL-GS interactions at the molecular level. The reduced density gradient (RDG) along with the calculated isosurfaces asserts that the dominant interactions are noncovalent interactions. Furthermore, the enzymology of cytochrome-c in the aqueous SAIL-GS aggregated systems has been investigated and a two-fold increase in the enzyme activity has been observed in the aggregates formed by the GS as compared to that in buffer
Beschreibung:Date Revised 22.08.2023
published: Print-Electronic
Citation Status PubMed-not-MEDLINE
ISSN:1520-5827
DOI:10.1021/acs.langmuir.3c01050