Binding of an anticancer drug, axitinib to human serum albumin: Fluorescence quenching and molecular docking study

Tayyab, Saad; Izzudin, Mohamad Mirza; Kabir, Md. Zahirul; Feroz, Shevin Rizal; Tee, Wei-Ven; Mohamad, Saharuddin Bin; Alias, Zazali

doi:10.1016/j.jphotobiol.2016.06.049

Cited by 78 publications

(40 citation statements)

References 45 publications

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“…MEF‐induced decline in the FI at 343 nm of HSA (Figure A) was suggestive of MEF binding to HSA as well as presence of Trp‐214 at or near the MEF‐binding site. This was akin to several earlier reports showing similar quenching pattern upon drug binding to protein . Additionally, the small blue shift in the emission maxima can be ascribed either to the hydrophobic changes in the microenvironment around Trp residue upon MEF binding or due to relative increase in contribution from Tyr residues.…”

Section: Discussionsupporting

confidence: 86%

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Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches

et al. 2019

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The interaction between mefloquine (MEF), the antimalarial drug, and human serum albumin (HSA), the main carrier protein in blood circulation, was explored using fluorescence, absorption, and circular dichroism spectroscopic techniques. Quenching of HSA fluorescence with MEF was characterized as static quenching and thus confirmed the complex formation between MEF and HSA. Association constant values for MEF‐HSA interaction were found to fall within the range of 3.79‐5.73 × 104 M˗1 at various temperatures (288, 298, and 308 K), which revealed moderate binding affinity. Hydrogen bonds and hydrophobic interactions were predicted to connect MEF and HSA together in the MEF‐HSA complex, as deduced from the thermodynamic data (ΔS = +133.52 J mol−1 K−1 and ΔH = +13.09 kJ mol−1) of the binding reaction and molecular docking analysis. Three‐dimensional fluorescence spectral analysis pointed out alterations in the microenvironment around aromatic amino acid (tryptophan and tyrosine) residues of HSA consequent to the addition of MEF. Circular dichroic spectra of HSA in the wavelength ranges of 200‐250 and 250‐300 nm hinted smaller changes in the protein's secondary and tertiary structures, respectively, induced by MEF binding. Noncovalent conjugation of MEF to HSA bettered protein thermostability. Site marker competitive drug displacement results suggested HSA Sudlow's site I as the MEF binding site, which was also supported by molecular docking analysis.

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Section: Discussionsupporting

confidence: 86%

“…In line with the published procedure, increasing concentrations of MEF 3‐27 μM at 3 μM interval were used, while the concentration of HSA was kept at 3 μM. The total volume was made to 3 mL with PB 7.4.…”

Section: Methodsmentioning

confidence: 99%

Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches

et al. 2019

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“…These results suggested ground state stable complex formation between HSA and ligands . Furthermore, it confirmed that static quenching was the mechanism here, as dynamic quenching only changes the excited state of the fluorophore and has no effect on absorption spectra . Additionally, an unaffected λ max value (280 nm) supported the existence of noncovalent interactions such as π–π stacking between ligands and HSA …”

Section: Resultssupporting

confidence: 79%

Insight into the interaction of benzothiazole tethered triazole analogues with human serum albumin: Spectroscopy and molecular docking approaches

Yadav

Dixit³

et al. 2019

Luminescence

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The interaction of four benzothiazole tethered triazole analogues (MS43, MS70, MS71, and MS78) with human serum albumin (HSA) was investigated using various spectroscopic techniques (ultraviolet-visible (UV-vis) light absorption, fluorescence, circular dichroism (CD), molecular docking and density functional theory (DFT) studies). Fluorescence quenching constants (~10 12 ) revealed a static mode of quenching and binding constants (K b~1 0 4 ) indicating the strong affinity of these analogues for HSA. Further alteration in the secondary structure of HSA in the presence of these analogues was also confirmed by far UV-CD spectroscopy. The intensity loss in CD studied at 222 nm indicated an increase in random coil/β-sheet conformations in the protein. Binding energy values (MS71 (−9.3 kcal mol −1 ), MS78 (−8.02 kcal mol −1 ), MS70 (−7.16 kcal mol −1 ) and MS43 (−6.81 kcal mol −1 )) obtained from molecular docking revealed binding of these analogues with HSA. Molecular docking and DFT studies validated the experimental results, as these four analogues bind with HSA at site II through hydrogen bonding and hydrophobic interactions.

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“…The increase in K sv values with temperature was attributed to faster diffusion of fluorophore and quencher molecules at higher temperatures. This faster diffusion of molecules increased the interaction between the fluorophore and quencher and thereby increased the quenching constant . These observations, indicated the presence of dynamic quenching mechanism .…”

Section: Resultsmentioning

confidence: 70%

Interaction of Indole Derivative with Human Serum Albumin: A Combined Spectroscopic and Molecular Dynamics Study

2018

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In the present work, we have studied the interaction of synthesized indole derivative (ID) with a model protein, human serum albumin (HSA). Various spectroscopic and molecular dynamic simulation methods were employed to characterize the binding between ID and HSA. ID showed strong binding affinity towards HSA (1.86x106 M−1) and quenched the fluorescence intensity of HSA by dynamic quenching mechanism. The existence of dynamic quenching mechanism in ID‐HSA interaction was further confirmed by lifetime measurement study. ID‐HSA interaction was favored by hydrophobic forces. The binding site for ID on HSA was examined by site probe competitive experiments and molecular docking studies. The results revealed that ID was bound to HSA primarily at site I of subdomain IIA. Absorption, 3D fluorescence and circular dichroism (CD) studies provided information on the conformational and microenvironmental changes in HSA upon binding to ID.

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Binding of an anticancer drug, axitinib to human serum albumin: Fluorescence quenching and molecular docking study

Cited by 78 publications

References 45 publications

Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches

Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches

Insight into the interaction of benzothiazole tethered triazole analogues with human serum albumin: Spectroscopy and molecular docking approaches

Interaction of Indole Derivative with Human Serum Albumin: A Combined Spectroscopic and Molecular Dynamics Study

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