Fluorescence spectrometric study on the interactions of isoprocarb and sodium 2-isopropylphenate with bovine serum albumin
Ni, Yongnian, Liu, Genlan, & Kokot, Serge (2008) Fluorescence spectrometric study on the interactions of isoprocarb and sodium 2-isopropylphenate with bovine serum albumin. Talanta, 76(3), pp. 513-521.
The binding interaction of the pesticide Isoprocarb and its degradation product, sodium 2-isopropylphenate, with bovine serum albumin (BSA) was studied by spectrofluorimetry under simulated physiological conditions. Both Isoprocarb and sodium 2-isopropylphenate quenched the intrinsic fluorescence of BSA. This quenching proceeded via a static mechanism. The thermodynamic parameters (ΔH°, ΔS° and ΔG°) obtained from the fluorescence data measured at two different temperatures showed that the binding of Isoprocarb to BSA involved hydrogen bonds and that of sodium 2-isopropylphenate to BSA involved hydrophobic and electrostatic interactions. Synchronous fluorescence spectroscopy of the interaction of BSA with either Isoprocarb or sodium 2-isopropylphenate showed that the molecular structure of the BSA was changed significantly, which is consistent with the known toxicity of the pesticide, i.e., the protein is denatured. The sodium 2-isopropylphenate, was estimated to be about 4–5 times more toxic than its parent, Isoprocarb.
Synchronous fluorescence spectroscopy and the resolution of the three-way excitation–emission fluorescence spectra by the PARAFAC method extracted the relative concentration profiles of BSA, Isoprocab and sodium 2-isopropylphenate as a function of the added sodium 2-isopropylphenate. These profiles showed that the degradation product, sodium 2-isopropylphenate, displaced the pesticide in a competitive reaction with the BSA protein.
Impact and interest:
Citation counts are sourced monthly from and citation databases.
Citations counts from theindexing service can be viewed at the linked Google Scholar™ search.
|Item Type:||Journal Article|
|Keywords:||Isoprocarb, Sodium 2-isopropylphenate, Bovine serum albumin, Interactions, Three-way excitation–emission fluorescence|
|Subjects:||Australian and New Zealand Standard Research Classification > CHEMICAL SCIENCE (030000) > MEDICINAL AND BIOMOLECULAR CHEMISTRY (030400) > Medicinal and Biomolecular Chemistry not elsewhere classified (030499)
Australian and New Zealand Standard Research Classification > CHEMICAL SCIENCE (030000) > ANALYTICAL CHEMISTRY (030100)
Australian and New Zealand Standard Research Classification > CHEMICAL SCIENCE (030000) > ANALYTICAL CHEMISTRY (030100) > Analytical Spectrometry (030101)
|Divisions:||Past > QUT Faculties & Divisions > Faculty of Science and Technology
Past > Schools > School of Physical & Chemical Sciences
|Copyright Owner:||Copyright 2008 Elsevier BV|
|Deposited On:||02 Dec 2009 00:45|
|Last Modified:||29 Feb 2012 13:43|
Repository Staff Only: item control page