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 countsare sourced monthly fromand citation databases.
These databases contain citations from different subsets of available publications and different time periods and thus the citation count from each is usually different. Some works are not in either database and no count is displayed. Scopus includes citations from articles published in 1996 onwards, and Web of Science® generally from 1980 onwards.
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 10:45|
|Last Modified:||29 Feb 2012 23:43|
Repository Staff Only: item control page