Molecular binding mechanism of 5-hydroxy-1-methylpiperidin-2-one with human serum albumin

Yadav, Sangilimuthu Alagar; Yeggoni, Daniel Pushparaju; Devadasu, Elsinraju; Subramanyam, Rajagopal

doi:10.1080/07391102.2017.1300106

Cited by 9 publications

(8 citation statements)

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“…Where F cor and F obs are corrected and observed fluorescence intensity respectively. A ext and A emi are absorbance at fluorescence excitation (285 nm) and emission (360 nm) wavelengths [ 28 ]. To validate whether the complex is undergoing dynamic or static quenching, bimolecular quenching constant was calculated from the slope of F O /F vs Q and it was found to be linear, which indicates that it is undergoing static quenching.…”

Section: Resultsmentioning

confidence: 99%

“…Using site specific markers we can understand the exact binding of ligand molecules to the specific domains of HSA. Hence, there are different site specific markers like lidocaine for domain I, phenylbutazone for domain II and ibuprofen for domain III [ 22 ] and using these markers the fluorescence was performed to analyze the specific binding domain of HSA on interaction with withanoside and withanolide derivatives [ 28 , 31 ]. Because of the structural and molecular similarity of four derivatives, all of them showed fluorescence emission quenching by displacing phenylbutazone, i.e.…”

Section: Resultsmentioning

confidence: 99%

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Elucidating the active interaction mechanism of phytochemicals withanolide and withanoside derivatives with human serum albumin

et al. 2018

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Withania somnifera (Ashwagandha) is an efficient medicinal plant known in Ayurveda and Chinese medicine since ancient times, whose extracts are consumed orally as food supplement or as a health tonic owing to its several restorative properties for various CNS disorders, inflammation, tumour, stress, rheumatism etc. In this study, we have analyzed the binding interaction of four derivatives of Withania somnifera (Withanolide A, Withanolide B, Withanoside IV and Withanoside V) with HSA because of their important pharmacological properties. To unravel the binding between derivatives of Withania somnifera and HSA, fluorescence spectroscopy was used. Binding studies were further studied by molecular docking and dynamics and results confirmed greater stability upon binding of derivatives with HSA. Circular dichroism data illustrated change in the secondary structure of protein upon interaction with these derivatives, particularly the helical structure was increased and β-sheets and random coils were decreased. Furthermore, morphological and topological changes were observed using AFM and TEM upon binding of ligands with HSA indicating that HSA-withnoside/withanolide complexes were formed. All the results cumulatively demonstrate strong binding of withanosides and withanolides derivatives with serum albumin, which should further be explored to study the pharmacokinetics and pharmacodynamics of these derivatives.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Elucidating the active interaction mechanism of phytochemicals withanolide and withanoside derivatives with human serum albumin

et al. 2018

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Section: Fluorescence Spectroscopymentioning

confidence: 99%

“…Using site specific markers we can understand the exact binding of ligand molecules to the specific domains of HSA. Hence, there are different site specific markers like lidocaine for domain I, phenylbutazone for domain II and ibuprofen for domain III [22] and using these markers the fluorescence was performed to analyze the specific binding domain of HSA on interaction with withanoside and withanolide derivatives [28,32]. Kcal M -1 respectively (Fig 2 A-D).…”

Section: Displacement Studiesmentioning

confidence: 99%

“…This plant is known to be found globally, with more occurrences in xeric and drier regions of tropical and subtropical areas [2,3]. We have selected four derivatives of this plant, which are withanolide A (C 28 activities like chemopreventive, anti-inflammatory, anti-arthritic, and angiogenesis activity [4], and they are being used as a rasayana to promote immunity,health and longevity which acts as a adaptogen and immunomodulator. These compounds are also known to exhibit nootropic effect and are effective against several neurodegenerative diseases including Alzheimer's and Parkinson's disease [5], hence Ashwagandha derivatives have become very popular oral supplement globally because of its strong remedial properties.…”

Section: Introductionmentioning

confidence: 99%

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Elucidating the active interaction mechanism of phytochemicals withanolide and withanoside derivatives with human serum albumin

Dubey

Kallubai

Sarkar

et al. 2018

Preprint

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Withania somnifera (Ashwagandha) is an efficient plant known in Ayurveda and Chinese medicine since ancient times, whose extracts are consumed orally as food supplement or as a health tonic owing to its several restorative properties for various CNS disorders, inflammation, tumour, stress and rheumatism. In this study, we have analyzed the binding interaction of four derivatives of Withania somnifera (Withanolide A, Withanolide B, Withanoside IV and Withanoside V) with HSA because of their important pharmacological properties. To unravel the binding between derivatives of Withania somnifera and HSA,fluorescence spectroscopy was used .Binding studies were further studied by molecular docking and dynamics studies and results confirmed greater stability upon binding of derivatives with HSA. Circular dichroism data illustrated change in the secondary structure of protein upon interaction with these derivatives, particularly the helical structure was increased and β-sheets and random coils were decreased .Furthermore, morphological and topological changes were observed using AFM and TEM upon binding of ligands with HSA indicating that HSA-withnoside/withanolide complexes were formed. All the results cumulatively demonstrate strong binding of withanosides and withanolides derivatives with serum albumin, which should further be explored to study the pharmacokinetics and pharmacodynamics of these derivatives.

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Experimental and computational studies on the binding of diazinon to human serum albumin

Jafari

Samadi

Nowroozi

et al. 2017

Journal of Biomolecular Structure and Dynamics

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In the present research, the binding properties of diazinon (DZN), as an organophosphorus herbicide, to human serum albumin (HSA) were investigated using combination of spectroscopic, electrochemistry, and molecular modeling techniques. Changes in the UV-Vis and FT-IR spectra were observed upon ligand binding along with a significant degree of tryptophan fluorescence quenching on complex formation. The obtained results from spectroscopic and electrochemistry experiments along with the computational studies suggest that DZN binds to residues located in subdomains IIA of HSA with binding constant about 1410.9 M at 300 K. From the thermodynamic parameters calculated according to the van't Hoff equation, the enthalpy change ΔH° and entropy change ΔS° were found to be -16.695 and 0.116 KJ/mol K, respectively. The primary binding pattern is determined by hydrophobic interaction and hydrogen binding occurring in so-called site I of HSA. DZN could slightly alter the secondary structure of HSA. All of experimental results are supported by computational techniques such as docking and molecular dynamics simulation using a HSA crystal model.

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Molecular binding mechanism of 5-hydroxy-1-methylpiperidin-2-one with human serum albumin

Cited by 9 publications

References 10 publications

Elucidating the active interaction mechanism of phytochemicals withanolide and withanoside derivatives with human serum albumin

Elucidating the active interaction mechanism of phytochemicals withanolide and withanoside derivatives with human serum albumin

Elucidating the active interaction mechanism of phytochemicals withanolide and withanoside derivatives with human serum albumin

Experimental and computational studies on the binding of diazinon to human serum albumin

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