The interrelationship between ligand binding and self-association of the folate binding protein. The role of detergent-tryptophan interaction

Holm, Jan; Schou, Christian; Nygren Babol, Linnea; Lawaetz, Anders J.; Bruun, Susanne W.; Hansen, Morten Z.; Hansen, Steen I.

doi:10.1016/j.bbagen.2011.07.005

Abstract

General significance: Self-association into multimers may protect binding sites, and in case of holo-FBP even folate from biological degradation. High-affinity folate binding in body secretions, typically containing 1-10 nM FBP, requires the presence of natural detergents, i.e. cholesterol and phospholipids, to avoid complexation between apo- and holo-FBP. (C) 2011 Elsevier B.V. All rights reserved.

Keywords

Folate binding protein; Ligand mediated self-association; Asymmetric apo-holo complexes; Surface plasmon resonance; Detergent-tryptophan interaction; Fluorescence spectroscopy

Published in

Biochimica et biophysica acta G. General subjects
2011, volume: 1810, number: 12, pages: 1330-1339
Publisher: ELSEVIER SCIENCE BV

SLU Authors

Nygren Babol, Linnea
- Department of Molecular Sciences, Swedish University of Agricultural Sciences

UKÄ Subject classification

Biochemistry
Biophysics
Molecular Biology

Publication identifier

DOI: https://doi.org/10.1016/j.bbagen.2011.07.005

Permanent link to this page (URI)

https://res.slu.se/id/publ/46025