Journal of Fluorescence

, Volume 18, Issue 1, pp 75–85

Fluorescence Characterization of the Hydrophobic Pocket of Cyclophilin B

Authors

    • Laboratoire de Biophysique MoléculaireUniversité des Sciences et Technologies de Lille, Bât. C6
  • M. Carpentier
    • Unité de Glycobiologie structurale et fonctionnelle, UMR n° 8576Université des Sciences et Technologies de Lille
  • C. Lansiaux
    • Laboratoire de Biophysique MoléculaireUniversité des Sciences et Technologies de Lille, Bât. C6
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

Abstract

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.

Keywords

Cyclophilin BTrp residues2-p-toluidinylnaphthalene-6-sulfonate (TNS)Red-edge excitation spectraFluorescence anisotropyFluorescence lifetimesQuantum yieldEmission to excitation ratio

Abbreviations

a.u.

arbitrarily scaled units

CsA

cyclosporin A

hCyPB

human cyclophilin B

Copyright information

© Springer Science+Business Media, LLC 2007