Study of jack bean urease interaction with luteolin by the extended solvation model and docking simulation

In this study, the interaction between Luteolin and urease was made at 300 K in aqueous buffer solutions using isothermal titration calorimetry. The extended solvation model was used to calculate the solvation parameters. Moreover, to determine the interaction of Luteolin with Jack Bean Urease (JBU)...

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Veröffentlicht in:AIMS Biophysics 2020-01, Vol.7 (4), p.429-435
Hauptverfasser: Mazinani, Maryam, Rezaei Behbehani, Gholamreza, Gheibi, Nematollah, Farasat, Alireza
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Sprache:eng
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Zusammenfassung:In this study, the interaction between Luteolin and urease was made at 300 K in aqueous buffer solutions using isothermal titration calorimetry. The extended solvation model was used to calculate the solvation parameters. Moreover, to determine the interaction of Luteolin with Jack Bean Urease (JBU), a molecular docking process was performed. The purpose of this investigation was to measure the inhibitory effects of Luteolin on the activity and structure of urease. Molecular docking analysis confirmed the extended solvation model. Keywords: Isothermal Titration Calorimetry; luteolin; the extended solvation theory; inhibitor; docking
ISSN:2377-9098
2377-9098
DOI:10.3934/biophy.2020029