Effect of urea on serum albumin complex with antithyroid drugs: fluorescence study

Sułkowska, Anna; Bojko, Barbara; Równicka, J.; Pentak, Danuta; Sułkowski, Wieslaw W.

doi:10.1016/s0022-2860(02)00635-x

Cited by 56 publications

(34 citation statements)

References 11 publications

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“…Studies on the stabilization induced by different chemical agents are of considerable importance. [14][15][16][17]21,[57][58][59] We performed a study on the stabilization effect of a NSAID, the ibuprofen. To verify the protective action of the ibuprofen, an analysis with SAXS, DLS, CD and fluorescence techniques was carried out on a set of solutions with urea concentrations between 0.00 and 9.00 M.…”

Section: Discussionmentioning

confidence: 99%

Human serum albumin binding ibuprofen: A 3D description of the unfolding pathway in urea

Galantini¹,

Leggio²,

Konarev³

et al. 2010

Biophysical Chemistry

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT2 AbstractSmall angle X-ray scattering (SAXS) technique, supported by light scattering measurements and spectroscopic data (circular dichroism and fluorescence) allowed us to restore the 3D structure at low resolution of defatted human serum albumin (HSA) in interaction with ibuprofen. The data were carried out on a set of HSA solutions with urea concentrations between 0.00 and 9.00 M. The SingularValue Decomposition method, applied to the complete SAXS data set allowed us to distinguish three different states in solution. In particular a native conformation N (at 0.00 M urea), an intermediate I1(at 6.05 M urea) and an unfolded structure U (at 9.00 M urea) were recognized. The low resolution structures of these states were obtained by exploiting both ab initio and rigid body fitting methods. In particular, for the protein without denaturant, a conformation recently described (Leggio & al., PCCP, 2008, 10, 6741-6750), very similar to the crystallographic heart shape, with only a slight reciprocal movement of the three domains, was confirmed. The I1 structure was instead characterized by only a closed domain (domain III) and finally, the recovered structure of the U state revealed the characteristic feature of a completely open state. A direct comparison with the free HSA pointed out that the presence of the ibuprofen provokes a shift of the equilibrium towards higher urea concentrations without changing the unfolding sequence. The work represents a type of analysis which could be exploited in future investigations on proteins in solution, in the binding of drugs or endogenous compounds and in the pharmacokinetic properties as well as in the study of allosteric effects, cooperation or anticooperation mechanisms.

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Section: Discussionmentioning

confidence: 99%

Human serum albumin binding ibuprofen: A 3D description of the unfolding pathway in urea

Galantini¹,

Leggio²,

Konarev³

et al. 2010

Biophysical Chemistry

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“…It can bind a wide variety of ligands such as bilirubin, fatty acids, hematin, surfactants and drugs [1][2][3][4][5][6][7][8][9]. Studies on the binding mechanism between protein and small molecules can give us a lot of useful information.…”

Section: Introductionmentioning

confidence: 99%

Quenching of the intrinsic fluorescence of bovine serum albumin by phenylfluorone–Mo(VI) complex as a probe

Wu¹,

Wei²,

Li³

et al. 2005

International Journal of Biological Macromolecules

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“…In almost all life processes, proteins are very important. They interact with a wide variety of surfactants, drugs and ligands such as bilirubin, fatty acids, hematin and metal ions [53][54][55][56][57][58][59][60][61][62][63]. Due to the applications in biosciences, foods and cosmetics, drug delivery, detergents and biotechnological process interactions of proteins with surfactants have been studied for many years.…”

Section: Surfactant-amino Acid Interactionsmentioning

confidence: 99%

Surfactant–Amino Acid and Surfactant–Surfactant Interactions in Aqueous Medium: a Review

Malik

2015

Appl Biochem Biotechnol

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An overview of surfactant-amino acid interactions mainly in aqueous medium has been discussed. Main emphasis has been on the solution thermodynamics and solute-solvent interactions. Almost all available data on the topic has been presented in a lucid and simple way. Conventional surfactants have been discussed as amphiphiles forming micelles and amino acids as additives and their effect on the various physicochemical properties of these conventional surfactants. Surfactant-surfactant interactions in aqueous medium, various mixed surfactant models, are also highlighted to assess their interactions in aqueous medium. Finally, their applied part has been taken into consideration to interpret their possible uses.

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Effect of urea on serum albumin complex with antithyroid drugs: fluorescence study

Cited by 56 publications

References 11 publications

Human serum albumin binding ibuprofen: A 3D description of the unfolding pathway in urea

Human serum albumin binding ibuprofen: A 3D description of the unfolding pathway in urea

Quenching of the intrinsic fluorescence of bovine serum albumin by phenylfluorone–Mo(VI) complex as a probe

Surfactant–Amino Acid and Surfactant–Surfactant Interactions in Aqueous Medium: a Review

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