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Publication Detail
Ligand-dependent conformational equilibria of serum albumin revealed by tryptophan fluorescence quenching
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Chadborn N, Bryant J, Bain AJ, O'Shea P
  • Publication date:
    01/01/1999
  • Pagination:
    2198, 2207
  • Journal:
    Biophysical Journal
  • Volume:
    76
  • Issue:
    4
  • Status:
    Published
  • Print ISSN:
    0006-3495
Abstract
Ligand-dependent structural changes in serum albumin are suggested to underlie its role in physiological solute transport and receptor-mediated cellular selection. Evidence of ligand-induced (oleic acid) structural changes in serum albumin are shown in both time-resolved and steady-state fluorescence quenching and anisotropy measurements of tryptophan 214 (Trpa ). These studies were augmented with column chromatography separations. It was found that both the steady-state and time-resolved Stern- Volmer collisional quenching studies of Trp with acrylamide pointed to the existence of an oleate-dependent structural transformation. The bimolecular quenching rate constant of defatted human serum albumin, 1.96 x 10 M s , decreased to 0.94 x 10 M s after incubation with oleic acid (9:1). Furthermore, Stern-Volmer quenching studies following fractionation of the structural forms by hydrophobic interaction chromatography were in accordance with this interpretation. Time-resolved fluorescence anisotropy measurements of the Trp residue yielded information of motion within the protein together with the whole protein molecule. Characteristic changes in these motions were observed after the binding of oleate to albumin. The addition of oleate was accompanied by an increase in the rotational diffusion time of the albumin molecule from ~22 to 33.6 ns. Within the body of the protein, however, the rotational diffusion time for Trp exhibited a slight decrease from 191 to 182 ps and was accompanied by a decrease in the extent of the angular motion of Trp , indicating a transition after oleate binding to a more spatially restricted but less viscous environment. 214 214 9 -1 -1 9 -1 -1 214 214 214
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