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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.


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.


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

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

Publication Identifiers


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