Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies

Naik, Keerti M.; Kolli, Deepa B; Nandibewoor, Sharanappa T.

doi:10.1186/2193-1801-3-360

Cited by 26 publications

(13 citation statements)

References 29 publications

(37 reference statements)

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“…Dynamic quenching and static quenching can be distinguished by their different dependence upon the temperature of quenching constants or viscosity, or by lifetime measurements [11] , [12] . The quenching rate constants decreased with increased temperature for static quenching, but the reverse effect is observed in the case of dynamic quenching [13] . In both cases, molecular contact is required between the flurophore and the quencher for fluorescence quenching [14] .…”

Section: Resultsmentioning

confidence: 84%

Multi-spectroscopic characterization of bovine serum albumin upon interaction with atomoxetine

Buddanavar

Nandibewoor

2017

Journal of Pharmaceutical Analysis

115

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The quenching interaction of atomoxetine (ATX) with bovine serum albumin (BSA) was studied in vitro under optimal physiological condition (pH=7.4) by multi-spectroscopic techniques. The mechanism of ATX-BSA system was a dynamic quenching process and was confirmed by the fluorescence spectra and lifetime measurements. The number of binding sites, binding constants and other binding characteristics were computed. Thermodynamic parameters ∆H° and ∆S° indicated that intermolecular hydrophobic forces predominantly stabilized the drug-protein system. The average binding distance between BSA and ATX was studied by Försters theory. UV-absorption, Fourier transform infrared spectroscopy (FT-IR), circular dichroism (CD), synchronous spectra and three-dimensional (3D) fluorescence spectral results revealed the changes in micro-environment of secondary structure of protein upon the interaction with ATX. Displacement of site probes and the effects of some common metal ions on the binding of ATX with BSA interaction were also studied.

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Section: Resultsmentioning

confidence: 84%

Multi-spectroscopic characterization of bovine serum albumin upon interaction with atomoxetine

Buddanavar

Nandibewoor

2017

Journal of Pharmaceutical Analysis

115

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“…HSA has three intrinsic fluorophores: tryptophan (Trp), tyrosine (Tyr) and phenylalanine (Phe) and changes in HSA fluorescence are associated with its interaction or binding to a variety of quenchers. [62][63][64][65] As observed in Figure 2A, HSA fluorescence emission decreases with increasing concentrations of AntiOxCIN 3 , with a shift to higher wavelengths (from 334 to 352 nm). Emission spectral shifts can be used to estimate the surrounding hydrophobicity of the chromophore, since the fluorescence emission is strongly dependent on the local microenvironment.…”

Section: Results and Discussion Interaction Studies With Micelles Modmentioning

confidence: 54%

Lipid Nanosystems and Serum Protein as Biomimetic Interfaces: Predicting the Biodistribution of a Caffeic Acid-Based Antioxidant

Fernandes

Benfeito

Cagide

et al. 2021

NSA

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AntiOxCIN 3 is a novel mitochondriotropic antioxidant developed to minimize the effects of oxidative stress on neurodegenerative diseases. Prior to an investment in preclinical in vivo studies, it is important to apply in silico and biophysical cell-free in vitro studies to predict AntiOxCIN 3 biodistribution profile, respecting the need to preserve animal health in accordance with the EU principles (Directive 2010/63/EU). Accordingly, we propose an innovative toolbox of biophysical studies and mimetic models of biological interfaces, such as nanosystems with different compositions mimicking distinct membrane barriers and human serum albumin (HSA). Methods: Intestinal and cell membrane permeation of AntiOxCIN 3 was predicted using derivative spectrophotometry. AntiOxCIN 3-HSA binding was evaluated by intrinsic fluorescence quenching, synchronous fluorescence, and dynamic/electrophoretic light scattering. Steady-state and time-resolved fluorescence quenching was used to predict AntiOxCIN 3membrane orientation. Fluorescence anisotropy, synchrotron small-and wide-angle X-ray scattering were used to predict lipid membrane biophysical impairment caused by AntiOxCIN 3 distribution. Results and Discussion: We found that AntiOxCIN 3 has the potential to permeate the gastrointestinal tract. However, its biodistribution and elimination from the body might be affected by its affinity to HSA (>90%) and by its steady-state volume of distribution (VD SS =1.89 ± 0.48 L•Kg −1). AntiOxCIN 3 is expected to locate parallel to the membrane phospholipids, causing a bilayer stiffness effect. AntiOxCIN 3 is also predicted to permeate through blood-brain barrier and reach its therapeutic target-the brain. Conclusion: Drug interactions with biological interfaces may be evaluated using membrane model systems and serum proteins. This knowledge is important for the characterization of drug partitioning, positioning and orientation of drugs in membranes, their effect on membrane biophysical properties and the study of serum protein binding. The analysis of these interactions makes it possible to collect valuable knowledge on the transport, distribution, accumulation and, eventually, therapeutic impact of drugs which may aid the drug development process.

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“…On the contrary, the effect is usually reversed with static quenching, i. e . the quenching constant shrinkage with increased temperature due to the formation of a ground state complex with the protein . In the case of fluorescence quenching, the molecular proximity is necessary in both cases, between the fluorophore and quencher .…”

Section: Resultsmentioning

confidence: 99%

Synthesisand Characterization of Benzothiophene‐3‐carbonitrile Derivative and Its Interactions with Human Serum Albumin (HSA)

et al. 2019

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A series of biologically active compounds, i. e., benzothiophene‐3‐carbonitrile derivatives, were synthesized from 1,3‐cyclohexanediones and malononitrile in the presence of base using the well‐known Gewald reaction. This recyclable approach resulted in significant improvement in overall yield (85‐90%), high purity and minimized production of chemical waste without using toxic reagents. The formation of compound, 2‐amino‐7‐oxo‐4,5,6,7‐tetrahydro‐1‐benzothiophene‐3‐carbonitrile (3 a) was additionally supported by X‐ray crystallography and was found to crystallize in P21/n space group. The mode of binding of 3 a with human serum albumin (HSA) was studied by FTIR, UV spectroscopy, fluorescence spectroscopy, circular dichroism (CD) and molecular docking studies. The fluorescence results establish that compound 3 a interacted with HSA via static quenching mechanism with a binding affinity of 11.49 × 10−4 mol−1 and Gibbs free energy change (ΔG) of−6.8 kcal mol−1. Molecular docking has been used to calculate the probable mode of interaction of compound 3 a with HSA.

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Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies

Cited by 26 publications

References 29 publications

Multi-spectroscopic characterization of bovine serum albumin upon interaction with atomoxetine

Multi-spectroscopic characterization of bovine serum albumin upon interaction with atomoxetine

Lipid Nanosystems and Serum Protein as Biomimetic Interfaces: Predicting the Biodistribution of a Caffeic Acid-Based Antioxidant

Synthesisand Characterization of Benzothiophene‐3‐carbonitrile Derivative and Its Interactions with Human Serum Albumin (HSA)

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