Supramolecular interaction of 6-shogaol, a therapeutic agent of Zingiber officinale with human serum albumin as elucidated by spectroscopic, calorimetric and molecular docking methods

Feroz, Shevin Rizal; Mohamad, Sharifah; Lee, G.S.; Malek, Sri Nurestri Abd; Tayyab, Saad

doi:10.1016/j.phymed.2015.03.016

Cited by 27 publications

(5 citation statements)

References 53 publications

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“…Change in the physical property such as thermal stability of a protein upon ligand addition has also been considered as indirect evidence of ligand‐protein interaction . In agreement to this notion, increased thermostability of HSA in the presence of ligands have been demonstrated in several earlier reports . Using decline in the FI signal at 342 nm as the probe for thermal destabilization of HSA, lesser decrease in the fluorescence signal with the MEF as related to that obtained with protein alone (Figure C) clearly pointed out thermal stabilization of HSA upon MEF addition.…”

Section: Discussionsupporting

confidence: 77%

“…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%

“…Due to higher sensitivity and micromolar concentration requirement, fluorescence spectroscopy has become the popular technique to study ligand‐protein interactions . In many cases, ligand‐induced quenching of protein's fluorescence has been suggested as the evidence for ligand binding to protein . The interaction studies between several antimalarial drugs and serum albumins have been published, based on fluorescence and other spectroscopic techniques .…”

Section: Discussionmentioning

confidence: 99%

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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: 77%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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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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“…These interactions are reversible and vary with the amounts of individual proteins and corresponding substances. Serum components constantly undergo small conformational changes as a result of interactions between the various molecules 35,36 . Hydrogen nuclei exist under a diverse array of conditions that are closely related to the supramolecular structure and physical serum properties.…”

Section: Discussionmentioning

confidence: 99%

Short-time Fourier Transform of Free Induction Decays for the Analysis of Serum Using Proton Nuclear Magnetic Resonance

et al. 2019

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Serum is the liquid portion of blood routinely used as a clinical specimen. Serum consists of low-molecular-weight compounds 1 3 , macromolecules and their degradation products 4, 5 , inorganic ions 6, 7 , and water. Hydrogen nuclei in serum play important roles through intra-and intermolecular interactions with other nuclei. Most of the hydrogen atoms in serum are associated with water molecules or proteins. Water molecules form hydrogen bonds with nitrogen and hydrogen atoms in macromolecules and low-molecular-weight compounds, stabilizing their molecular conformations 8 11. Hydrogen bonding also takes place in the interactions between solutes. Thus, serum has its own dynamic features and assumes a supramolecular structure

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“…Such quenching in the fluorescence intensity indicated the binding of nandrolone decanoate to HSA, and suggested that the polarity changes in the microenvironment around Trp residue might be responsible for the observed quenching of the fluorescence intensity observed. [34][35][36][37] Fluorescence quenching of the single tryptophan residue in HSA was used to measure drug-binding affinity. Tryptophan fluorescence is the most frequently examined among the three intrinsic aromatic fluorophores in HSA molecules to obtain information about conformational changes.…”

Section: Interaction Of Nandrolone Decanoate Drug With Hsa In Presmentioning

confidence: 99%

Enhanced Transport of Nandrolone Decanoate Drug by Human Serum Albumin in Presence of [BMIM]PF6 and [BMIM]BF4

Yasseen

Saadeh

Shawish

2018

ACSi

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The interaction of nandrolone decanoate drug dissolved in (2%) [BMIM]BF 4 or [BMIM]PF 6 with human serum albumin (HSA) at different temperatures in the range of 285-310 K was examined by fluorescence quenching. Stern-Volmer equation and its modified form were used to determine the interaction parameters K and n. The results revealed that binding affinities of HSA for nandrolone decanoate drug in 2% [BMIM]BF 4 or [BMIM]PF 6 are in the order of 10 5 M-1 and the number of bound drug molecules per HSA macromolecule are approximated to 1 at all temperatures studied. The thermodynamic parameters: free energy change (∆G o), enthalpy change (∆H o) and entropy change (∆S o) for HSAnandrolone decanoate/ionic liquid were calculated according to van't Hoff equation. Data analysis indicated that both electrostatic interactions and hydrophobic ineractions played important roles in the interaction of nandrolone decanoate drug with HSA.

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Supramolecular interaction of 6-shogaol, a therapeutic agent of Zingiber officinale with human serum albumin as elucidated by spectroscopic, calorimetric and molecular docking methods

Cited by 27 publications

References 53 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

Short-time Fourier Transform of Free Induction Decays for the Analysis of Serum Using Proton Nuclear Magnetic Resonance

Enhanced Transport of Nandrolone Decanoate Drug by Human Serum Albumin in Presence of [BMIM]PF6 and [BMIM]BF4

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