Study of the Interactions of Bovine Serum Albumin with the New Anti-Inflammatory Agent 4-(1,3-Dioxo-1,3-dihydro-2H-isoindol-2-yl)-N′-[(4-ethoxy-phenyl)methylidene]benzohydrazide Using a Multi-Spectroscopic Approach and Molecular Docking

Wani, Tanveer A.; Bakheit, Ahmed H.; Al-Majed, Abdulhakeem A.; Bhat, Mashooq A.; Zargar, Seema

doi:10.3390/molecules22081258

Cited by 55 publications

(33 citation statements)

References 26 publications

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“…mdb output file was generated for further analysis and evaluation of neratinib–BSA interaction. The active binding site that might be involved in the interaction was obtained from the site specific probe experiments (Jahanban-Esfahlan et al, 2015 ; Wani et al, 2017b , c ). RMSD (root mean square deviation) parameters were used to select the most suitable interaction of BSA with neratinib.…”

Section: Methodsmentioning

confidence: 99%

“…Plasma proteins act as carriers for transportation of drugs and other compounds. Amongst the various plasma proteins, serum albumin is the most abundant protein and it plays a vital role in transportation of drug ligands (Jahanban-Esfahlan et al, 2015 ; Wani et al, 2017b , c ). Several tyrosine kinase inhibitors have been studied for their interaction with bovine serum protein (BSA) (Shen et al, 2015 ) and in this study, the interaction of neratinib with BSA was explored.…”

Section: Introductionmentioning

confidence: 99%

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Study of Interactions of an Anticancer Drug Neratinib With Bovine Serum Albumin: Spectroscopic and Molecular Docking Approach

et al. 2018

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Binding of therapeutic agents to plasma proteins, particularly to serum albumin, provides valuable information in the drug development. This study was designed to evaluate the binding interaction of neratinib with bovine serum albumin (BSA). Neratinib blocks HER2 signaling and is effective in trastuzumab-resistant breast cancer treatment. Spectrofluorometric, UV spectrophotometric, and fourier transform infrared (FT-IR) and molecular docking experiments were performed to study this interaction. The fluorescence of BSA is attributed to the presence of tryptophan (Trp) residues. The fluorescence of BSA in presence of neratinib was studied using the excitation wavelength of 280 nm and the emission was measured at 300-500 nm at three different temperatures. Neratinib quenched the BSA intrinsic fluorescence by static mechanism. A complex formation occurred due to the interaction leading to BSA absorption shift. The fluorescence, UV- absorption, three dimensional fluorescence and FT-IR data showed conformational changes occurred in BSA after interaction with neratinib. The binding constant values decreased as the temperature increased suggesting an instable complex formation at high temperature. Site I (sub-domain IIA) was observed as the principal binding site for neratinib. Hydrogen bonding and Van der Waals forces were suggested to be involved in the BSA-neratinib interaction due to the negative values of entropy and enthalpy changes.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Study of Interactions of an Anticancer Drug Neratinib With Bovine Serum Albumin: Spectroscopic and Molecular Docking Approach

et al. 2018

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“…Synchronous Fluorescence Studies. Synchronous fluorescence studies provide information regarding the microenvironmental changes in the amino acids responsible for fluorescence of protein [44][45][46][47]. ese studies measure the shift in the λ em, which might have occurred due to variations near the chromophores of a molecule.…”

Section: Conformational Studiesmentioning

confidence: 99%

“…Molecular docking helps to understand and interpret the interaction mechanism between BSA and 5d [47,49,50]. Molecular docking acts as an insilico tool to analyze the protein-ligand interaction and authenticate experimental interpretations.…”

Section: Molecular Dockingmentioning

confidence: 99%

Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

Almehizia

Bakheit

Zargar

et al. 2019

Journal of Spectroscopy

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In this research, the pyrazoline pyridazine derivative 7-methyl-2-phenyl-4-(3,4,5-trimethoxyphenyl)-2H-pyrazolo[3,4-d]pyridazine (5d) was studied for its interaction with bovine serum albumin (BSA). Various spectroscopic techniques along with molecular docking analysis were utilized to understand the mechanism of interaction. The quenching of BSA fluorescence by using investigational drug 5d was the basic principle for the methodology. Spectrofluorometric methods and UV-absorption studies were conducted for exploration of the 5d and BSA binding mechanism. The fluorescence quenching mechanism involved in BSA and 5d interaction was static quenching, and a complex formation also occurred between them. Both enthalpy and entropy attained positive values suggesting involvement of hydrophobic forces in BSA and 5d interaction. The Förster distance of 2.23 nm was calculated by fluorescence resonance energy transfer (FRET). An alteration in BSA secondary structure was proven from the conformational studies of BSA-5d interaction. This binding interaction study provided a basis to comprehend the binding interaction between 5d and BSA. These results provided information about sites of BSA involved in its interaction with 5d.

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“…Serum albumin binds to various ligands (hormones, fatty acids, drugs etc), thus playing a significant role in the pharmacokinetic behavior of these ligands 6. The therapeutic efficiency of the ligands depend on their ability to bind to BSA and the mechanism involved in the binding 7–11. Bovine serum albumin is commonly substituted for human serum albumin due to its structural similarity, low procurement cost, and availability.…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic and molecular modeling studies of binding interaction between bovine serum albumin and roflumilast

Wani¹,

Bakheit²,

Ansari³

et al. 2018

DDDT

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BackgroundThe binding interaction between bovine serum albumin (BSA) and roflumilast (ROF) was explored in this study. The binding of drugs to albumin plays a vital role in their pharmacokinetics and pharmacodynamics in vivo. The mechanisms involved in the interaction between BSA and ROF was studied using multi-spectroscopic experimental and computational approaches.Materials and methodsSpectrofluorometric experiments were used to determine the method of quenching involved and the conformational changes in the BSA. UV–visible spectroscopy synchronous and three-dimensional fluorescence spectroscopy were used to further explore the binding interaction mechanism.ResultsThe results suggested that the intrinsic fluorescence of BSA was quenched due to the formation of a static complex between ROF and BSA. Conformational changes in BSA were determined based on its interaction with ROF. The thermodynamic results suggested that the interaction between ROF and BSA was spontaneous and a hydrophobic interaction occurred between them. Site I of BSA was suggested as the site of interaction between ROF and BSA based on the site marker experiments.ConclusionThe molecular simulation results and the experimental outcomes were complimentary to each other and helped to identify the binding site and nature of bonds involved in the interaction between ROF and BSA.

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Study of the Interactions of Bovine Serum Albumin with the New Anti-Inflammatory Agent 4-(1,3-Dioxo-1,3-dihydro-2H-isoindol-2-yl)-N′-[(4-ethoxy-phenyl)methylidene]benzohydrazide Using a Multi-Spectroscopic Approach and Molecular Docking

Cited by 55 publications

References 26 publications

Study of Interactions of an Anticancer Drug Neratinib With Bovine Serum Albumin: Spectroscopic and Molecular Docking Approach

Study of Interactions of an Anticancer Drug Neratinib With Bovine Serum Albumin: Spectroscopic and Molecular Docking Approach

Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

Spectroscopic and molecular modeling studies of binding interaction between bovine serum albumin and roflumilast

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