Proton magnetic resonance studies of the aggregation of taurine-conjugated bile salts.

Journal Article (Journal Article)

The concentration dependence of the 500 MHz 1H-NMR spectra of taurocholate, taurochenodeoxycholate, taurodeoxycholate, and the monosulfate esters of taurochenodeoxycholate has been examined at 0.154 M NaCl in D2O. The resonances of the C18, C19, and C21 methyl groups and the C23 methylene group are differentially broadened with respect to the C25 and C26 methylene and C7 (or C12) methine groups with increasing bile salt concentration for each of the bile salts studied. These data confirm hydrophobic association and indicate that the side chain contributes to the hydrophobic surface of the bile salt. The chemical shift difference of the anisochronous C23 methylene protons is different in monomer and aggregate form. The C25 methylene protons are isochronous in monomeric form but anisochronous in aggregate form. The concentration dependence of the observed chemical shifts has been analyzed to estimate the critical concentration associated with the onset of these changes. The conformer population about the C22-C23 bond changes before the anisochronicity of the C25 methylene protons develops. This indicates that the C23 methylene group is affected by the initial stages of self-association, whereas specific motional constraints about the N-C25 bond in the taurine moiety are only induced in large primary micelles. The difference in the chemical shift of the C25 methylene protons depends on the structure of the bile salt. The relative magnitude of the shift differences is not altered by the presence of phosphatidylcholine. The data suggest that in primary micelles or mixed micelles the taurine moiety conforms to segregate the hydrophilic groups of the bile salt and effects greater van der Waals' contact between the hydrophobic surfaces.

Full Text

Duke Authors

Cited Authors

  • Stevens, RD; Ribeiro, AA; Lack, L; Killenberg, PG

Published Date

  • January 1992

Published In

Volume / Issue

  • 33 / 1

Start / End Page

  • 21 - 29

PubMed ID

  • 1552230

International Standard Serial Number (ISSN)

  • 0022-2275


  • eng

Conference Location

  • United States