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

Maryam Mazinani; Gholamreza Rezaei Behbehani; Nematollah Gheibi; Alireza Farasat; Maryam Mazinani; Gholamreza Rezaei Behbehani; Nematollah Gheibi; Alireza Farasat

doi:10.3934/biophy.2020029

AIMS Biophysics

2020, Volume 7, Issue 4: 429-435. doi: 10.3934/biophy.2020029

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

1.
Department of Chemistry, Imam Khomeini International University, Qazvin, Iran
2.
Department of Cell and Molecular Sciences, Cellular and Molecular Research Center, Qazvin University

Received: 16 July 2020 Accepted: 26 September 2020 Published: 12 October 2020

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.
- Isothermal Titration Calorimetry,
- luteolin,
- the extended solvation theory,
- inhibitor,
- docking
Citation: Maryam Mazinani, Gholamreza Rezaei Behbehani, Nematollah Gheibi, Alireza Farasat. Study of jack bean urease interaction with luteolin by the extended solvation model and docking simulation[J]. AIMS Biophysics, 2020, 7(4): 429-435. doi: 10.3934/biophy.2020029

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Abstract

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.

Conflict of interest

The authors declare no conflict of interest.

References

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