Urea-Induced Denaturation Process on Defatted Human Serum Albumin and in the Presence of Palmitic Acid

Leggio, Claudia; Galantini, Luciano; Konarev, Petr V.; Pavel, Nicolae Viorel

doi:10.1021/jp904330v

Cited by 47 publications

(56 citation statements)

References 67 publications

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“…For DF-HSA the helix content falls from 54% to about 37% . This resultis consistent with the denaturation results of Leggio et al [15]that the fatty acids in F-HSA confer structural stability and hence resistance to nanoparticle-induced denaturation and the conformation changes of human hemoglobin seen on silica [16].…”

Section: Protein Secondary Structure Changessupporting

confidence: 93%

Interaction of Human Serum Albumin and Silica at the air-water interface

Ang¹,

Lin²,

Yaron³

et al. 2014

IOSRJAP

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Section: Protein Secondary Structure Changessupporting

confidence: 93%

Interaction of Human Serum Albumin and Silica at the air-water interface

Ang¹,

Lin²,

Yaron³

et al. 2014

IOSRJAP

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“…By comparing the interpretation of the spectroscopic and the scattering data of the HSAIbu system with the results obtained for the free HSA defatted solutions 21 it was clear that in the case of the HSAIbu, the unfolding process takes place later on the denaturant concentration scale. Indeed, we observed that the HSA binding ibuprofen molecules remained in the native form up to a limit urea concentration of 3.90 M. This limit value is higher than the one reported for HSA (2.50 M).…”

Section: Discussionmentioning

confidence: 88%

“…21 A very detailed analysis of SAXS, DLS, CD and fluorescence was carried out. In particular, the SVD analysis and the three-dimensional reconstructions allowed the determination of number, percentage and low resolution structures of the conformers involved in the unfolding process.…”

Section: Resultsmentioning

confidence: 99%

“…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%

“…We performed a study on the HSA:ibuprofen complex at various urea concentrations and we compared it with the free HSA denaturation in the same conditions. 21 The comparison, besides establishing the ibuprofen stabilization activity, can help us in the definition of the domain opening sequence in the structure reconstruction, thus further clarifying the albumin unfolding mechanism.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

See 2 more Smart Citations

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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Comparative Study of Flavins Binding with Human Serum Albumin: A Fluorometric, Thermodynamic, and Molecular Dynamics Approach

et al. 2012

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Flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) are derivatives of riboflavin (RF), a water-soluble vitamin, more commonly known as vitamin B(2). Flavins have attracted special attention in the last few years because of the recent discovery of a large number of flavoproteins. In this work, these flavins are used as extrinsic fluorescence markers for probing the microheterogeneous environment of a well-known transport protein, human serum albumin (HSA). Steady-state and time-resolved fluorescence experiments confirm that both FMN and FAD bind to the Sudlow's site-1 (SS1) binding pocket of HSA, where Trp214 resides. In the case of RF, a fraction of RF molecules binds at the SS1, whereas the major fraction of RF molecules remains unbound or surface bound to the protein. Moreover, flavin(s)-HSA interactions are monitored with the help of isothermal titration calorimetry, which provides free energy, enthalpy, and entropy changes of binding along with the binding constants. The molecular picture of binding interaction between flavins and HSA is well explored by docking and molecular dynamics studies.

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Urea-Induced Denaturation Process on Defatted Human Serum Albumin and in the Presence of Palmitic Acid

Cited by 47 publications

References 67 publications

Interaction of Human Serum Albumin and Silica at the air-water interface

Interaction of Human Serum Albumin and Silica at the air-water interface

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

Comparative Study of Flavins Binding with Human Serum Albumin: A Fluorometric, Thermodynamic, and Molecular Dynamics Approach

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