A Structural and Calorimetric Study on the Interaction Between Jack Bean Urease and Cyanide Ion

Behbehani, G. Rezaei; Saboury, Ali Akbar; Mohebbian, M.; Tahmasebi, Sanaz; Poorheravi, Mohammad R.

doi:10.1007/s10953-009-9471-7

Cited by 5 publications

(6 citation statements)

References 30 publications

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“…In 2009 we identified more than 400 articles after searching Web of Science, PubMed, SciDir and OVID databases using ‘isothermal AND titration AND calorimetry’ or ITC or ‘Isothermal Titration Calorimetry’ search terms. These have been classified into the following categories: Pre‐2009 references cited in the text and review articles 1–43 Protein‐protein and protein‐peptide interactions 44–124 Protein/peptide‐small molecule interactions 125–218 Protein/peptide‐metal ion interactions 219–253 Protein/peptide‐nucleic acid interactions 254–273 Protein/peptide‐lipid interactions 274–292 Protein/peptide‐polysaccharide interactions 293–316 Nucleic acid‐small molecule interactions 317–348 Small molecule interactions …”

Section: Introductionmentioning

confidence: 99%

Survey of the year 2009: applications of isothermal titration calorimetry

Falconer

Collins

2010

J. Mol. Recognit.

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Isothermal titration calorimetry (ITC) is now an established and invaluable method for determining the thermodynamic constants, association constant and stoichiometry of molecular interactions in aqueous solutions. The technique has become widely used by biochemists to study protein interaction with other proteins, small molecules, metal ions, lipids, nucleic acids and carbohydrates; and nucleic acid interaction with small molecules. The drug discovery industry has utilized this approach to measure protein (or nucleic acid) interaction with drug candidates. ITC has been used to screen candidates, guide the design of potential drugs and validate the modelling used in structure-based drug design. Emerging disciplines including nanotechnology and drug delivery could benefit greatly from ITC in enhancing their understanding and control of nano-particle assembly, and drug binding and controlled release.

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Section: Introductionmentioning

confidence: 99%

Survey of the year 2009: applications of isothermal titration calorimetry

Falconer

Collins

2010

J. Mol. Recognit.

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“…Meanwhile, the total binding free energy obtained from ITC and extended solvation model was almost close to the MMPBSA result, as shown in Table 2 and 3. Finally, comparing the results of MD with the previous study, it can be seen that the solubility extended solvation model (Behbehani et al, 2009;Behbehani et al, 2016;Behbehani & Barzegar, 2013;Poursoleiman et al, 2019;Rezaei Behbehani, Saboury, Mohebbian, et al, 2010). On many enzymes and inhibitors used in vitro is a successful model that, along with molecular dynamics and simulation, can help researchers in medicine and enzymes and physicians and patients.…”

Section: Simulations and Mm-pbsa Analysismentioning

confidence: 82%

Molecular dynamics simulations, molecular docking, and kinetics study of kaempferol interaction on Jack bean urease: Comparison of extended solvation model

Zolghadr

Behbehani

Pakbin

et al. 2022

Food Science & Nutrition

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Since the urease enzyme creates gastric cancer, peptic ulcer, hepatic coma, and urinary stones in millions of people worldwide, it is essential to find strong inhibitors to help patients. Natural products are well known for their beneficial effects on health and efforts are being made to isolate the ingredients, the so-called flavonoids. Flavonoids are now considered as an indispensable component in a variety of nutraceutical, pharmaceutical, and cosmetic applications. Kaempferol (KPF) is an antioxidant found in many fruits and vegetables. Many reports have explained the significant effects of dietary KPF in reducing the risk of chronic diseases such as cancer, ischemia, stroke, and Parkinson's. The current study aimed at investigating the inhibitory impact of KPF on Jack bean urease (JBU) using molecular dynamics (MD) simulations and molecular mechanics Poisson-Boltzmann surface area (MM-PBSA) calculations to confirm the results obtained from isothermal titration calorimetry (ITC), extended solvation model, and docking software. In addition, UV-VIS spectrophotometry was used to study the kinetics of urease inhibition. Calorimetric and spectrophotometric determinations of the kinetic parameters of this inhibition indicate the occurrence of a reversible and noncompetitive mode. Also, the docking and MD results indicated that the urease had well adapted to the kaempferol in the binding pocket, thereby forming a stable complex. Kaempferol displayed low binding energy during MMPBSA calculations. The inhibitory potential of kaempferol was confirmed by experimental and simulation data, but in vivo investigations are also recommended to validate our results.

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“…The extended solvation model [15][16][17][18], which is applicable, in principle, to a variety of protein + ligand systems, was used to analyze the heats of interaction of MT + II and MT + I mixtures using the following equations:…”

Section: Resultsmentioning

confidence: 99%

“…Among the various dithiocarbamates, we tried to elucidate the effect of pphenylene-bis and phenyl dithiocarbamate ( Fig. 1) on mushroom tyrosinase stability at 27 and 37°C, applying the extended solvation model for the data analysis [15][16][17][18].…”

Section: Introductionmentioning

confidence: 99%

Inhibitory Effects of p-Phenylene-bis and Phenyl Dithiocarbamate on Mushroom Tyrosinase

et al. 2012

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The binding properties and structural changes of mushroom tyrosinase enzyme, MT, due to its interactions with phenyl dithiocarbamate (I) and p-phenylene-bis dithiocarbamate (II), were investigated at 27 and 37°C in phosphate buffer (10 mmol·L −1 ) at pH = 6.8 by isothermal titration calorimetric (ITC). The extended solvation model was used to calculate the solvation parameters, which were attributed to the stability of this enzyme. Thermodynamic analysis indicated that the predominant mode of interaction was hydrophobic in the binding of compound I to MT, while the binding of II to MT essentially depends on electrostatic interactions. It seems that II is a more potent MT inhibitor due to its two charged head groups that are able to chelate copper ions in the active enzyme site. It was concluded that MT has two distinct sites for p-phenylene-bis and phenyl dithiocarbamate.

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A Structural and Calorimetric Study on the Interaction Between Jack Bean Urease and Cyanide Ion

Cited by 5 publications

References 30 publications

Survey of the year 2009: applications of isothermal titration calorimetry

Survey of the year 2009: applications of isothermal titration calorimetry

Molecular dynamics simulations, molecular docking, and kinetics study of kaempferol interaction on Jack bean urease: Comparison of extended solvation model

Inhibitory Effects of p-Phenylene-bis and Phenyl Dithiocarbamate on Mushroom Tyrosinase

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