Title of article
Study of protein–probe complexation equilibria and protein–surfactant interaction using charge transfer fluorescence probe methyl ester of N,N-dimethylamino naphthyl acrylic acid Review Article
Author/Authors
Subrata Mahanta، نويسنده , , Rupashree Balia Singh، نويسنده , , Arnab Bagchi، نويسنده , , Debnarayan Nath، نويسنده , , Nikhil Guchhait، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2010
Pages
10
From page
917
To page
926
Abstract
In this paper, we demonstrate the interaction between intramolecular charge transfer (ICT) probe—Methyl ester of N,N-dimethylamino naphthyl acrylic acid (MDMANA) with bovine serum albumin (BSA) using absorption and fluorescence emission spectroscopy. The nature of probe protein binding interaction, fluorescence resonance energy transfer from protein to probe and time resolved fluorescence decay measurement predict that the probe molecule binds strongly to the hydrophobic cavity of the protein. Furthermore, the interaction of the anionic surfactant sodium dodecyl sulphate (SDS) with water soluble protein BSA has been investigated using MDMANA as fluorescenece probe. The changes in the spectral characteristics of charge transfer fluorescence probe MDMANA in BSA–SDS environment reflects well the nature of the protein–surfactant binding interaction such as specific binding, non-cooperative binding, cooperative binding and saturation binding.
Keywords
Bovine Serum Albumin (BSA) , Sodium dodecyl sulphate (SDS) , Fluorescence probe , N-dimethylamino naphthyl acrylic acid (MDMANA) , Methyl ester of N , Charge transfer
Journal title
Journal of Luminescence
Serial Year
2010
Journal title
Journal of Luminescence
Record number
1259997
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