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Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
Fluorescence Dynamics of Monocyclodextrin- and Bis(thiol-cyclodextrin)-Coumarin C153 Complexes
Marianna Gregova Trencanova1, Eduard Jane2, Vojtech Szocs3
1Department of Physical and Theoretical Chemistry, Comenius University, Mlynska dolina, Bratislava (Slovakia). trencanova@fns.uniba.sk.
Abstract:
The solvation and confinement of coumarin C153 within supramolecular host/guest complexes based on β-cyclodextrin (β-CD) and 6-deoxy-6-thio-β-cyclodextrin (β-CD-SH) in water are studied by fluorescence spectroscopy. For β-CD/C153, the 1:1 complex is proposed, and for β-CD-SH/C153 both the 1:1 and 2:1 complexes are believed to be formed. The 2:1 β-CD-SH/C153 complex has an association constant of 4.2×10(5) M(-1) and a C153 population of 82 %, which are interestingly high values, indicating that the proposed β-CD-SH dimers structure are connected by covalent disulfide bonds; this is supported by mass spectrometry. Solvation related to fast hydrogen-bond rearrangement as a part of fluorescence relaxation is determined by the ultrafast components of time-resolved spectroscopy to be 3 and 7 ps for the 1:1 β-CD/C153 and 2:1 β-CD-SH/C153 complexes, respectively.
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