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Search: WFRF:(Sennato Simona) > (2015)

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1.
  • Gubitosi, Marta, et al. (author)
  • Tailoring Supramolecular Nanotubes by Bile Salt Based Surfactant Mixtures.
  • 2015
  • In: Angewandte Chemie (International edition). - : Wiley. - 1521-3773. ; 54:24, s. 7018-7021
  • Journal article (peer-reviewed)abstract
    • An approach for tailoring self-assembled tubular structures is described. By controlling the relative composition of a two-component surfactant mixture comprising the natural bile salt lithocholate and its bolamphiphilic derivative, it was possible to finely tune the nanotube cross-section of the mixed tubular aggregates that self-associated spontaneously in aqueous solution at pH 12. The diameter was found to vary up to 50 % when the stoichiometric ratio of the two bile salts was changed. The tuning of supramolecular nanochannels with such remarkable precision is of significant interest for technological applications of these materials.
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2.
  • Travaglini, Leana, et al. (author)
  • A tryptophan-substituted cholic acid : expanding the family of labelled biomolecules
  • 2015
  • In: Colloids and Surfaces A: Physicochemical and Engineering Aspects. - : Elsevier BV. - 0927-7757. ; 483:Online 31 March 2015, s. 142-149
  • Journal article (peer-reviewed)abstract
    • The synthesis of a novel cholic acid derivative bearing in the C-3 position a residue of tryptophan linked through an amide bond is herein described. Acidic or basic conditions are needed for the solubilization of the derivative in water. In alkaline solutions the molecule shows a self-association similar to the one of its natural precursor leading to the formation of ellipsoidal micelles which does not involve significant Trp–Trp interactions. On the contrary, in acidic conditions strong interactions between the tryptophan moieties occur, leading to the formation of a gel at low temperature. These interactions are broken upon heating and small micelles similar to those observed at high pH are formed. In both cases, fluorescence spectra suggest a polar environment for the amino acid fluorophore not remarkably affected by the self-assembly.
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