Journal of Fluorescence

, Volume 18, Issue 1, pp 75–85

Fluorescence Characterization of the Hydrophobic Pocket of Cyclophilin B

Original Paper

DOI: 10.1007/s10895-007-0239-4

Cite this article as:
Albani, J.R., Carpentier, M. & Lansiaux, C. J Fluoresc (2008) 18: 75. doi:10.1007/s10895-007-0239-4


Human cyclophilin B is a monomeric protein that contains two tryptophan residues, Trp104 and 128. Trp128-residue belongs to the binding site of cyclosporin A and is the homologous of Trp 121 in CyPA, while Trp104 residue belongs to the hydrophobic pocket. In the present work, we studied the dynamics of Trp residue(s) of cyclophilin B and of the CyPBw128A mutant and of TNS-mutant complex. Our results showed that Trp-104 and TNS show restricted motions within their environments and that energy transfer between the two fluorophores is occurring.


Cyclophilin B Trp residues 2-p-toluidinylnaphthalene-6-sulfonate (TNS) Red-edge excitation spectra Fluorescence anisotropy Fluorescence lifetimes Quantum yield Emission to excitation ratio 



arbitrarily scaled units


cyclosporin A


human cyclophilin B

Copyright information

© Springer Science+Business Media, LLC 2007

Authors and Affiliations

  1. 1.Laboratoire de Biophysique MoléculaireUniversité des Sciences et Technologies de Lille, Bât. C6Villleneuve d’Ascq CédexFrance
  2. 2.Unité de Glycobiologie structurale et fonctionnelle, UMR n° 8576Université des Sciences et Technologies de LilleVilleneuve d’Ascq CédexFrance

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