Exploring the binding mechanism of Guaijaverin to human serum albumin: Fluorescence spectroscopy and computational approach

Caruso, Ícaro Putinhon; Vilegas, Wagner; Fossey, Marcelo Andrés; Cornélio, Marinônio Lopes

doi:10.1016/j.saa.2012.06.043

Cited by 34 publications

(15 citation statements)

References 32 publications

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“…The negative value of δG • (-39.43) reveals that the binding of Pd(II) complex to HSA is a spontaneous intermolecular reaction (41,49). This result is in agreement with results fromUV-Vis experiments.…”

Section: Binding Constant and Binding Sitessupporting

confidence: 89%

“…K q is the bimolecular quenching constant, τ 0 is the lifetime of the fluorophore in the absence of quencher and its value for HSA is 10 −8 s, [L] is the concentration of the quencher and K SV is the Stern-Volmer quenching constant (41). The above equation can be applied to determine K SV by linear regression of a plot of F 0 /F against [L] (42).…”

Section: Fluorescence Quenching Mechanism Of Hsa By the Palladium (Iimentioning

confidence: 99%

“…where F(λ) is the corrected fluorescence intensity of the donor in the wavelength range from λ to λ + λ, and ε(λ) is the extinction coefficient of the acceptor at λ (41). In order to obtain the distance between the donor (HSA) and the acceptor (Pd(II) complex) the concentrations of both are set to 4.2 × 10 −6 M. The overlap of the absorbance spectrum of the Pd(II) complex with the emission spectra of HSA is shown in Figure 9.…”

Section: Energy Transfer Between Pd(ii) Complex and Hsamentioning

confidence: 99%

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Investigation of the Binding Behavior between the S-heterocyclic Aromatic Palladium(II) Complex and Human Serum Albumin: Spectroscopic Approach

Saeidifar

Khanlarkhani

Eslami-Moghaddam

et al. 2015

Polycyclic Aromatic Compounds

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The interaction of 1, 10-phenanthroline octhyldithiocarbamato palladium(II) nitrate ([Pd(Oct-dtc)(phen)]NO 3 ) with human serum albumin (HSA) has been investigated by various spectroscopic techniques under physiological conditions. Here, HSA was titrated with the Pd(II) complex, followed by UV-Vis absorption spectroscopy to estimate a binding constant (K b ) and other thermodynamic parameters. The results indicate that the Pd (II) complex has a high affinity for bind HSA. Thermodynamic analysis showed that the enthalpy ( H • ) and entropy changes ( S • ) are positive and Gibbs free energy change ( G • ) is negative which indicated that hydrophobic interactions played the predominant role in the binding process. Fluorescence spectroscopy were used to show the mechanism and binding parameters of this interaction. Utilizing the Stern-Volmer equation, the Pd(II) complex quenched the intrinsic fluorescence of HSA via a static quenching procedure. The specific binding distances between the tryptophan (donor) proteins and Pd(II) complex (acceptor) were estimated by Forster resonance energy transfer. The CD results also showed the conformational changes on serum albumin upon binding with the Pd(II) complex.

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Section: Binding Constant and Binding Sitessupporting

confidence: 89%

Section: Fluorescence Quenching Mechanism Of Hsa By the Palladium (Iimentioning

confidence: 99%

Section: Energy Transfer Between Pd(ii) Complex and Hsamentioning

confidence: 99%

See 1 more Smart Citation

Investigation of the Binding Behavior between the S-heterocyclic Aromatic Palladium(II) Complex and Human Serum Albumin: Spectroscopic Approach

Saeidifar

Khanlarkhani

Eslami-Moghaddam

et al. 2015

Polycyclic Aromatic Compounds

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“…In the two subdomains, site I (in subdomain IIA) and site II (in subdomain IIIA) have important effects in binding to small molecules. HSA has been widely used as a model protein for many biochemical studies using fluorescence quenching .…”

Section: Introductionmentioning

confidence: 99%

Studies on the interactions of 3,6‐diaminoacridine derivatives with human serum albumin by fluorescence spectroscopy

2014

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This study reports the preparation and investigation of the modes of binding of the two symmetric 3,6-diaminoacridine derivatives obtained from proflavine, which are 3,6-diphenoxycarbonyl aminoacridine and 3,6-diethoxycarbonyl aminoacridine to human serum albumin (HSA). The interaction of HSA with the derivatives was investigated using fluorescence quenching and ultraviolet-visible absorption spectra at pH 7.2 and different temperatures. The results suggest that the derivatives used can interact strongly with HSA and are the formation of HSA-derivative complexes and hydrophobic interactions as the predominant intermolecular forces in stabilizing for each complex. The Stern-Volmer quenching constants, binding constants, binding sites and corresponding thermodynamic parameters ΔH, ΔS and ΔG were calculated at different temperatures. The binding distance (r) ~ 3 nm between the donor (HSA) and acceptors (3,6-diethoxycarbonyl aminoacridine, 3,6-diphenoxycarbonyl aminoacridine and proflavine) was obtained according to Förster's non-radiative energy transfer theory. Moreover, the limit of detection and limit of quantification of derivatives were calculated in the presence of albumin.

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“…Understand the interaction between drugs and the plasma proteins is essential because this binding affects their pharmacodynamic and pharmacokinetic properties and can make us understand the absorption and distribution of drug [13].A wide variety of biophysical methods have been used for the analysis of the interactions between protein and ligands, such as, fluorescence spectroscopy [14], fluorescence resonance energy transfer (FRET) [15,16],nuclear magnetic resonance (NMR) [17],isothermal titration calorimetry (ITC) [18], besides computational methods/ molecular modeling [19].…”

Section: Introductionmentioning

confidence: 99%

Investigation of the Interaction between Coumarins and Its Derivatives with Human Serum Albumin: STD-NMR, Fluorescence and Docking Molecular Studies

Souza¹,

Benzatti²,

Caruso³

et al. 2016

ijSciences

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Abstract:In this paper, binding interaction of Coumarin, including 4-Methylesculetin, Esculetin and Esculin, with human serum albumin (HSA) was investigated by using STD-NMR, fluorescence spectroscopy and molecular docking method. STD-NMR investigations indicated that the binding affinity sequence for HSA-ligands interaction was: 4-Methyllesculetin >Esculetin>Coumarin>Esculinbeingin accordance with the fluorescence studies. The molecular docking resultssuggested that coumarins and its derivatives were binding to HSA at subdomain IIA, nearby the Trp214 residue, which are consistent with the results of fluorescence quenching results. Overall, the experimental and theoretical data corroborate with each other and they are complementary.

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Exploring the binding mechanism of Guaijaverin to human serum albumin: Fluorescence spectroscopy and computational approach

Cited by 34 publications

References 32 publications

Investigation of the Binding Behavior between the S-heterocyclic Aromatic Palladium(II) Complex and Human Serum Albumin: Spectroscopic Approach

Investigation of the Binding Behavior between the S-heterocyclic Aromatic Palladium(II) Complex and Human Serum Albumin: Spectroscopic Approach

Studies on the interactions of 3,6‐diaminoacridine derivatives with human serum albumin by fluorescence spectroscopy

Investigation of the Interaction between Coumarins and Its Derivatives with Human Serum Albumin: STD-NMR, Fluorescence and Docking Molecular Studies

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