Journal
JOURNAL OF MOLECULAR STRUCTURE
Volume 963, Issue 2-3, Pages 122-129Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molstruc.2009.10.023
Keywords
Pentobarbital; HSA; Binding constant; Protein secondary structure; FT-IR spectroscopy
Categories
Funding
- German Research Foundation DFG [DR228/24-2]
Ask authors/readers for more resources
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 x 10(4) 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 alpha-helix relative to that of beta-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 alpha-helix and beta-sheets. (c) 2009 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available