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

Research article - Peer-reviewed, 2011

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.

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

Authors' information

Holm, Jan

Hillerød Hospital

Schou, Christian

Statens Serum Institut

Nygren Babol, Linnea

Swedish University of Agricultural Sciences, Department of Food Science

Lawaetz, Anders J.

University of Copenhagen

Bruun, Susanne W.

University of Copenhagen

Hansen, Morten Z.

Hansen, Steen I.

UKÄ Subject classification

Biochemistry and Molecular Biology
Biophysics

Publication Identifiers

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

URI (permanent link to this page)

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