Interactions between the antiviral drug telaprevir and human serum albumin: a combined study with spectroscopic methods and molecular modeling

Xiong, Xiaopeng; Gan, Ruixue; Suo, Zili; Tang, Peixiao; Zhang, Shuangshuang; Zhu, Ye; Sun, Qiaomei; Li, Hui

doi:10.1039/c8nj00655e

Cited by 16 publications

(12 citation statements)

References 42 publications

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“…Aforesaid binding affinity is important for adequate transport as well as release of the drug (MEF) at the target site upon circulation . Binding of many ligands including drugs to HSA have been reported with moderate binding affinity . Ligands/drugs can independently bind to any of the protein binding sites, each binding site has equal chance for the ligands/drugs to bind .…”

Section: Discussionmentioning

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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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: Discussionmentioning

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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“…Binding of drugs to plasma proteins is an imperative pharmacological aspect, because it affects the absorption, distribution, metabolism, and excretion properties of drug . Moreover, drug efficacy, stability, and toxicity in humans are also affected by binding to serum albumin . Therefore, the study of the mechanism of interaction between newer drug and serum albumin is helpful to obtain pharmacological properties of drug, which will help in further design of more effective drug candidates.…”

Section: Introductionmentioning

confidence: 99%

Interaction of coumarin triazole analogs to serum albumins: Spectroscopic analysis and molecular docking studies

Sharma

Yadav

Sharma

et al. 2020

J of Molecular Recognition

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The interaction of triazole substituted 4-methyl-7-hydroxycoumarin derivatives (CUM1-4) with serum albumin (bovine serum albumin [BSA] and human serum albumin[HSA]) have been studied employing ultraviolet-visible (UV-Vis), fluorescence, circular dichroism (CD) spectroscopy, and molecular docking methods at physiological pH 7.4.The fluorescence quenching occurred with increasing concentration of CUMs, and the binding constant of CUM derivatives with BSA and HSA obtained from fluorescence quenching experiment was found to be~10 4 L mol −1 . CD study showed conformational changes in the secondary structure of serum albumin upon titration of CUMs.The observed experimental results were further validated by theoretical studies involving density functional theory (DFT) and molecular docking. K E Y W O R D S circular dichroism, coumarin, fluorescence quenching, molecular docking, serum albumin

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“…This binding also affects its efficacy, stability, toxicity and delivery. 4 Thus, the study of the mechanism of the interaction between a drug and serum albumin is crucial to evaluate the transportation and distribution of the drug in the body. 3 Organic compounds containing chalcone and avone scaffolds are of interest to both synthetic and medicinal chemists.…”

Section: Introductionmentioning

confidence: 99%

Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches

Yadav

Agarwal

et al. 2019

RSC Adv.

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Interactions between the antiviral drug telaprevir and human serum albumin: a combined study with spectroscopic methods and molecular modeling

Abstract: The binding mechanism between telaprevir and human serum albumin was explored by combining spectroscopic methods and molecular dynamics simulations.

Cited by 16 publications

References 42 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

Interaction of coumarin triazole analogs to serum albumins: Spectroscopic analysis and molecular docking studies

Insights into the interaction of potent antimicrobial chalcone triazole analogs with human serum albumin: spectroscopy and molecular docking approaches

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