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Polymorphic Behavior in Protein-Surfactant Mixtures: The Water-Bovine SerumAlbumin-Sodium Taurodeoxycholate System

ORIONI B
•
ROVERSI M
•
LAMESA C
altro
D'ERRICO G.
2006
  • journal article

Periodico
JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL
Abstract
Mixtures containing water, bovine serum albumin (BSA), and sodium taurodeoxycholate (NaTDChave been investigated. Depending on the concentration of both solutes and the pH, solutions, precipitates, and gels are formed. At high concentrations, a gel, extending on both sides of the charge neutralization line, and two-phase regions are observed. The thermal gelation threshold, the temperature above which G> G, depends on BSA and NaTDC content and is concomitant to moderate heat effects, inferred by differential scanning calorimetry (DSC). Water self-diffusion in the gels is slightly slower than that in the bulk and poorly sensitive to composition: it is about 65% the value of neat H2O in a wide concentration range, irrespective of the BSA, or NaTDC, concentration. The 23Na T1 and T2 values, measured at 105.75 MHz on BSA-NaTDC gels, indicate that the motions determining the NMR relaxation of the sodium ions in the hydration layer of the protein-surfactant aggregates are not slow.
DOI
10.1021/jp055950r
WOS
WOS:000238284600076
Archivio
http://hdl.handle.net/11368/1700978
info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-33745800649
Diritti
metadata only access
Soggetti
  • gel

  • NMR relaxation

  • bile salt

Web of Science© citazioni
42
Data di acquisizione
Mar 28, 2024
Visualizzazioni
4
Data di acquisizione
Apr 19, 2024
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