Structural and functional changes of catalase through interaction with Erlotinib hydrochloride. Use of Chou's 5-steps rule to study mechanisms

Shahraki, Somaye; Delarami, Hojat Samareh; Poorsargol, Mahdiye; Nezami, Ziba Sori

doi:10.1016/j.saa.2021.119940

Cited by 23 publications

(11 citation statements)

References 63 publications

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“…Interaction of this drug with the antioxidant enzyme catalase and its inhibitory mechanism have been reported [5]. However, no study has been reported on the binding of Erlo to serum albumin proteins.…”

Section: Inhibition Of Epidermal Growth Factor Receptor Activity Is P...mentioning

confidence: 99%

“…This anticancer drug is also a kinase inhibitor. Erlo is used in the treatment of several types of cancers such as non-small-cell lung cancer and pancreatic cancer [5].…”

Section: Introductionmentioning

confidence: 99%

“…This anticancer drug is also a kinase inhibitor. Erlo is used in the treatment of several types of cancers such as non‐small‐cell lung cancer and pancreatic cancer [5]. Inhibition of epidermal growth factor receptor activity is possible with Erlo [6].…”

Section: Introductionmentioning

confidence: 99%

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Probing the combination of erlotinib hydrochloride, an anticancer drug, and human serum albumin: Spectroscopic, molecular docking, and molecular dynamic analyses

et al. 2023

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Human serum albumin (HSA) is a globular and monomeric protein in plasma that transports many drugs and compounds. Binding of some drugs to HSA can lead to changes in its stability and biological function. We investigated the binding interactions between erlotinib hydrochloride (Erlo) and HSA. Erlo is used to treat lung, pancreatic, and some other cancers. Experimental data showed that the fluorescence emission of the protein was quenched by Erlo using a static quenching mechanism. The calculation of the binding constant, K b (1.57 Â 10 5 M À1 at 300 K), confirmed the existence of a moderate binding interaction between Erlo and HSA.The interaction was enthalpy driven, spontaneous, and exothermic. The calculated thermodynamic parameters in agreement with simulation and molecular docking data showed that van der Waals and hydrogen bond forces played an important role in the interaction process. Molecular docking results indicated that Erlo has more affinity to bind to subdomain IIA (site I) of HSA. Molecular dynamics simulation analysis showed that the protein is stable in the presence of Erlo under simulation conditions.

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Section: Inhibition Of Epidermal Growth Factor Receptor Activity Is P...mentioning

confidence: 99%

“…This anticancer drug is also a kinase inhibitor. Erlo is used in the treatment of several types of cancers such as non-small-cell lung cancer and pancreatic cancer [5].…”

Section: Introductionmentioning

confidence: 99%

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Probing the combination of erlotinib hydrochloride, an anticancer drug, and human serum albumin: Spectroscopic, molecular docking, and molecular dynamic analyses

et al. 2023

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“…The interaction between small molecules and biomacromolecules, such as proteins, could be of various types, including hydrophobic interactions, electrostatic interactions, hydrogen bonding, and van der Waals forces. Moreover, the type of interaction force can be determined by the change in the values of thermodynamic parameters, including enthalpy (ΔH) and entropy (ΔS) (Shahraki et al, 2021). The thermodynamic parameters were calculated ac- 3 that the ΔG values for the binding process of cinnamaldehyde and citral to tyrosinase were both negatives, indicating that their binding processes to tyrosinase were spontaneous.…”

Section: Fluorescence Quenching Studiesmentioning

confidence: 99%

Composition analysis and tyrosinase inhibitory activity of Cinnamomum cassia Presl leaf hydrosol and Cymbopogon citratus ( DC .) Stapf leaf hydrosol

Duan

et al. 2022

Food Processing Preservation

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Hydrosol is a natural aromatic product possessing broad application prospects as a food preservative; however, limited information is available regarding its anti‐tyrosinase activity. Here, we investigated the inhibitory effects of Cinnamomum cassia Presl leaf hydrosol (CCPH) and Cymbopogon citratus (DC.) Stapf leaf hydrosol (CCSH) on tyrosinase activity. The primary components of CCPH and CCSH were cinnamaldehyde (82.1%) and citral (52.3%), respectively. The aromatic compound, terpenoid, and nitrogen oxide detectors within the electronic nose yielded higher response values for the two hydrosols. The IC50 values for CCPH, CCSH, cinnamaldehyde, and citral in regard to their effects on tyrosinase were 84.8 ± 15.5 (vol%), 23.9 ± 2.0 (vol%), 53.3 ± 10.7 mM, and 21.0 ± 6.5 mM, respectively. According to Lineweaver‐Burk plot analyses, cinnamaldehyde and citral are both non‐competitive inhibitors. Both CCPH and CCSH inhibited browning of mushrooms (Agaricus bisporus). These results suggest that hydrosols could be used as potential tyrosinase inhibitors in the food additive and cosmetic industries. Novelty impact statement The primary components of CCPH and CCSH were cinnamaldehyde (82.1%) and citral (52.3%), respectively. The hydrosols and their primary components exerted an inhibitory effect on tyrosinase. CCPH and CCSH could inhibit the browning of mushrooms (Agaricus bisporus).

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“…[4] Therefore, the study of the interaction of drugs and other chemicals on the structure and function of catalase can be significant. [5,6] Such studies would help clarify the mechanism of oxidative stress caused by some chemical compounds. Our research team seeks to investigate the interaction of metal complexes that can have drug potential with biomacromolecules.…”

Section: Introductionmentioning

confidence: 99%

A multidisciplinary study for investigating the interaction of an iron complex with bovine liver catalase

Hashemizadeh

Shiri

Shahraki

et al. 2022

Applied Organom Chemis

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Catalase (CAT) is an essential protein protecting the cell from oxidative damage by reactive oxygen species. CAT is a heme enzyme in which iron metal plays a crucial role in catalytic activity. In this research, an iron (II, III) complex ([Fe (bpy) 3 ] [Fe (dipic) 2 ] 2 .7H 2 O; dipic À2 = pyridine-2,6-dicarboxylato and bpy = 2,2 0 -bipyridine) was used to evaluate its binding interactions with bovine liver catalase (BLC) using spectroscopic and molecular docking methods. The experimental results demonstrated that the catalytic activity of BLC increased slightly and reached 106% of the initial activity. The interactions between Fe complex and BLC led to the quenching of the catalase fluorescence emission via the static quenching mechanism. Thermodynamic parameters demonstrated that the predominant interactions between catalase and Fe complex are hydrogen bond and van der Waals and the process is exothermic and enthalpy driven. The circular dichroism (CD) and synchronous fluorescence results showed that the Fe complex altered the structure and conformation of BLC. It changed the secondary structure of BLC by decreasing α-helix and β-sheet content. Also, the experimental data were analyzed using Multivariate Curve Resolution-Alternating Least Square (MCR-ALS) to the resolution of measured complex spectra and estimate the number of independent chemical species. The docking results in agreement with experimental data showed that the cationic part of the complex with catalase is mainly hydrophobic and van der Waals interactions, and for the anionic part are hydrophobic, van der Waals, and hydrogen bonding.

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Structural and functional changes of catalase through interaction with Erlotinib hydrochloride. Use of Chou's 5-steps rule to study mechanisms

Cited by 23 publications

References 63 publications

Probing the combination of erlotinib hydrochloride, an anticancer drug, and human serum albumin: Spectroscopic, molecular docking, and molecular dynamic analyses

Probing the combination of erlotinib hydrochloride, an anticancer drug, and human serum albumin: Spectroscopic, molecular docking, and molecular dynamic analyses

Composition analysis and tyrosinase inhibitory activity of Cinnamomum cassia Presl leaf hydrosol and Cymbopogon citratus ( DC .) Stapf leaf hydrosol

A multidisciplinary study for investigating the interaction of an iron complex with bovine liver catalase

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