3 research outputs found
Spectroscopic investigations of pentobarbital interaction with human serum albumin
The interaction between pentobarbital and human serum albumin has been investigated. The basic binding
interaction was studied by UV-absorption and fluorescence spectroscopy. From spectral analysis pentobarbital
showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching
procedure. The binding constant (k) is estimated at 1.812 104 M 1 at 293 K. FT-IR spectroscopy with
Fourier self-deconvolution technique was used to determine the protein secondary structure and drug
binding mechanisms. The observed spectral changes of HSA–pentobarbital complex indicate a larger
intensity decrease in the absorption band of a-helix relative to that of b-sheets. This variation in intensity
is related indirectly to the formation of H-bonding in the complex molecules, which accounts for the different
intrinsic propensities of a-helix and b-sheets.This work is supported by the German Research Foundation
DFG Grant No. DR228/24-2