Study of Progesterone interaction with Human Serum Albumin: Spectroscopic approach

Date
2011-01-17
Authors
Abu Teir, M. M.
Ghithan, J. H.
Darwish, S. M.
Abu-Hadid, M. M.
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Abstract
The interaction between progesterone and human serum albumin has been investigated. This interaction was studied by UV-absorption and fluorescence spectroscopy. From spectral analysis progesterone showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant (K) is estimated 6.56×102 M-1 at 293 K. FT-IR spectroscopy with Fourier self-deconvolution technique was used to determine HSA secondary structure and progesterone binding mechanisms. The observed spectral changes indicate the formation of H-bonding between progesterone and HSA molecules which can be related to the intensity decrease in the absorption band of α-helix relative to that of β-sheets.
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Keywords
progesterone, amide I-III, binding mode, binding constant, protein secondary structure, Fourier transform IR, UV–spectroscopy, Flurosence spectroscopy
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