Thermodynamic features of bile salt-human serum albumin interaction

Francesco Scagnolari, Aldo Roda, Adamo Fini, Brunella Grigolo

Research output: Contribution to journalArticlepeer-review


Interaction with human serum albumin is responsible for important aspects of the physiological behaviour of bile salts, although this factor has not been adequately examined. The nature of the binding is investigated here by means of thermodynamic parameters determined by equilibrium dialysis and microcalorimetric measurements. The positive enthalpy and entropy values obtained indicate the presence of a poorly specific hydrophobic bonding.

Original languageEnglish
Pages (from-to)274-277
Number of pages4
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number2
Publication statusPublished - Dec 7 1984


  • (Human serum)
  • Albumin-bile salt interaction
  • Bile salt
  • Cholate
  • Hydrophobic interaction

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology


Dive into the research topics of 'Thermodynamic features of bile salt-human serum albumin interaction'. Together they form a unique fingerprint.

Cite this