Size and polydispersity determinations of AOT/bile salt reversed micelles obtained by small-angle neutron scattering

Citation
Ks. Freeman et al., Size and polydispersity determinations of AOT/bile salt reversed micelles obtained by small-angle neutron scattering, LANGMUIR, 17(13), 2001, pp. 3912-3916
Citations number
26
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
LANGMUIR
ISSN journal
07437463 → ACNP
Volume
17
Issue
13
Year of publication
2001
Pages
3912 - 3916
Database
ISI
SICI code
0743-7463(20010626)17:13<3912:SAPDOA>2.0.ZU;2-H
Abstract
Previous work has shown that trihydroxy bile salt cosurfactants significant ly modify the interfacial properties and aggregate size of Aerosol-OT (AOT) reversed micelles and can also increase the activity of enzymes such as ch ymotrypsin and lipase that are solubilized in the AOT reversed micelles. In the present work, small-angle neutron scattering (SANS) was used to study the effects of one such bile salt, sodium taurocholate (NaTC), on the size and polydispersity of AOT reversed micelles. At low concentrations, NaTC de creases the overall size of the reversed micelles, the size of the interior water pools, and the apparent thickness of the detergent layer, while caus ing an increase in polydispersity. At higher NaTC concentrations, the overa ll aggregate size, the size of the water pools, the thickness of the deterg ent layer, and the polydispersity all are increased. It is proposed that, a t low concentrations, NaTC monomers are randomly dispersed among the AOT mo lecules in a perpendicular orientation, thereby disrupting the organization of the detergent layer and increasing penetration of heptane and water int o the detergent layer. When NaTC is increased, it may form hydrogen-bonded dimers that are aligned parallel to the AOT molecules. In this orientation, there is less disruption of the detergent layer and penetration of heptane and water molecules is reduced. Finally, it was found that reversed micell es containing chymotrypsin are smaller than unoccupied aggregates, suggesti ng structural reorganization in order to accommodate the protein. From thes e results, the effects of NaTC on chymotrypsin activity in AOT reversed mic elles can be attributed to structural and chemical modification of the dete rgent layer rather than to changes in the overall dimensions of the reverse d micelles.