albumin - publications

Predict more albumin - ligand interactions now!


1. Luminescence. 2012 Feb 7. doi: 10.1002/bio.2354. [Epub ahead of print]

Combining time-resolved fluorescence with synchronous fluorescence spectroscopy
to study bovine serum albumin-curcumin complex during unfolding and refolding
processes.

Barakat C, Patra D.

Department of Chemistry, American University of Beirut, Beirut, 1107-2020,
Lebanon.

We investigated the complex interaction between bovine serum albumin (BSA) and
curcumin by combining time-resolved fluorescence and synchronous fluorescence
spectroscopy. The interaction was significant and sensitive to fluorescence
lifetime and synchronous fluorescence characteristics. Binding of curcumin
significantly shortened the fluorescence lifetime of BSA with a bi-molecular
quenching rate constant of k(q)  = 3.17 × 10(12) M(-1) s(-1) . Denaturation by
urea unfolded the protein molecule by quenching the fluorescence lifetime of BSA.
The tyrosine synchronous fluorescence spectra were blue shifted whereas the
position of tryptophan synchronous fluorescence spectra was red shifted during
the unfolding process. However, denaturation of urea had little effect on the
synchronous fluorescence peak of tyrosine in curcumin-BSA complex except in the
low concentration range; however, it shifted the peak to the red, indicating that
curcumin shifted tryptophan moiety to a more polar environment in the unfolded
state. Decreases in the time-resolved fluorescence lifetime and curcumin-BSA
complex during unfolding were recovered during refolding of BSA by a dilution
process, suggesting partial reversibility of the unfolding process for both BSA
and curcumin-BSA complex. Copyright © 2012 John Wiley & Sons, Ltd.

Copyright © 2012 John Wiley & Sons, Ltd.

PMID: 22311564 [PubMed - as supplied by publisher]